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{{Infobox_gene}}
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'''Transcriptional enhancer factor TEF-1''' also known as '''TEA domain family member 1''' ('''TEAD1''') and '''transcription factor 13''' ('''TCF-13''') is a [[protein]] that in humans is encoded by the ''TEAD1'' [[gene]].<ref name="Xiao_1991">{{cite journal | vauthors = Xiao JH, Davidson I, Matthes H, Garnier JM, Chambon P | title = Cloning, expression, and transcriptional properties of the human enhancer factor TEF-1 | journal = Cell | volume = 65 | issue = 4 | pages = 551–68 | date = May 1991 | pmid = 1851669 | pmc =  | doi = 10.1016/0092-8674(91)90088-G }}</ref><ref name="pmid9889009">{{cite journal | vauthors = Jacquemin P, Depetris D, Mattei MG, Martial JA, Davidson I | title = Localization of human transcription factor TEF-4 and TEF-5 (TEAD2, TEAD3) genes to chromosomes 19q13.3 and 6p21.2 using fluorescence in situ hybridization and radiation hybrid analysis | journal = Genomics | volume = 55 | issue = 1 | pages = 127–9 | date = Jan 1999 | pmid = 9889009 | pmc =  | doi = 10.1006/geno.1998.5628 }}</ref><ref name="pmid15016762">{{cite journal | vauthors = Fossdal R, Jonasson F, Kristjansdottir GT, Kong A, Stefansson H, Gosh S, Gulcher JR, Stefansson K | title = A novel TEAD1 mutation is the causative allele in Sveinsson's chorioretinal atrophy (helicoid peripapillary chorioretinal degeneration) | journal = Human Molecular Genetics | volume = 13 | issue = 9 | pages = 975–81 | date = May 2004 | pmid = 15016762 | pmc =  | doi = 10.1093/hmg/ddh106 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TEAD1 TEA domain family member 1 (SV40 transcriptional enhancer factor)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7003| accessdate = }}</ref> TEAD1 was the first member of the TEAD family of [[transcription factor]]s to be identified.<ref name="Xiao_1991"/><ref name="ReferenceA">{{cite journal | vauthors = Mar JH, Ordahl CP | title = A conserved CATTCCT motif is required for skeletal muscle-specific activity of the cardiac troponin T gene promoter | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 85 | issue = 17 | pages = 6404–8 | date = September 1988 | pmid = 3413104 | doi=10.1073/pnas.85.17.6404 | pmc=281980}}</ref>
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| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[File:TEAD1Wiki figure.jpg|thumb|right]]
{{GNF_Protein_box
| image = PBB_Protein_TEAD1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2hzd.
| PDB = {{PDB2|2hzd}}
| Name = TEA domain family member 1 (SV40 transcriptional enhancer factor)
| HGNCid = 11714
| Symbol = TEAD1
| AltSymbols =; REF1; AA; TCF13; TEF-1
| OMIM = 189967
| ECnumber = 
| Homologene = 2418
| MGIid = 101876
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7003
    | Hs_Ensembl = ENSG00000187079
    | Hs_RefseqProtein = NP_068780
    | Hs_RefseqmRNA = NM_021961
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 12723164
    | Hs_GenLoc_end = 12922066
    | Hs_Uniprot = P28347
    | Mm_EntrezGene = 21676
    | Mm_Ensembl = ENSMUSG00000055320
    | Mm_RefseqmRNA = NM_009346
    | Mm_RefseqProtein = NP_033372
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 112470774
    | Mm_GenLoc_end = 112691171
    | Mm_Uniprot = Q3UFP5
  }}
}}
'''TEA domain family member 1 (SV40 transcriptional enhancer factor)''', also known as '''TEAD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TEAD1 TEA domain family member 1 (SV40 transcriptional enhancer factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7003| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Structure ==
{{PBB_Summary
| section_title =  
| summary_text =  
}}


==References==
All members of the TEAD family share a highly conserved DNA binding domain called the TEA domain.<ref>{{cite journal | vauthors = Hwang JJ, Chambon P, Davidson I | title = Characterization of the transcription activation function and the DNA binding domain of transcriptional enhancer factor-1 | journal = The EMBO Journal | volume = 12 | issue = 6 | pages = 2337–48 | date = June 1993 | pmid = 8389695 | pmc=413464}}</ref> This DNA binding domain has a consensus DNA sequence 5’-CATTCCA/T-3’ that is called the MCAT element.<ref>{{cite journal | vauthors = Farrance IK, Mar JH, Ordahl CP | title = M-CAT binding factor is related to the SV40 enhancer binding factor, TEF-1 | journal = The Journal of Biological Chemistry | volume = 267 | issue = 24 | pages = 17234–40 | date = August 1992 | pmid = 1324927 }}</ref> The three dimensional structure of the TEA domain has been identified [5]. Its conformation is close to that of the homeodomain and contains 3 α helixes (H1, H2 and H3). It is the H3 helix that enables TEAD proteins to bind DNA.<ref>{{cite journal | vauthors = Anbanandam A, Albarado DC, Nguyen CT, Halder G, Gao X, Veeraraghavan S | title = Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 103 | issue = 46 | pages = 17225–30 | date = November 2006 | pmid = 17085591 | doi = 10.1073/pnas.0607171103 | pmc=1859914}}</ref>
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Xiao JH, Davidson I, Matthes H, ''et al.'' |title=Cloning, expression, and transcriptional properties of the human enhancer factor TEF-1. |journal=Cell |volume=65 |issue= 4 |pages= 551-68 |year= 1991 |pmid= 1851669 |doi=  }}
*{{cite journal | author=Boam DS, Davidson I, Chambon P |title=A TATA-less promoter containing binding sites for ubiquitous transcription factors mediates cell type-specific regulation of the gene for transcription enhancer factor-1 (TEF-1). |journal=J. Biol. Chem. |volume=270 |issue= 33 |pages= 19487-94 |year= 1995 |pmid= 7642633 |doi= }}
*{{cite journal  | author=Fossdal R, Magnússon L, Weber JL, Jensson O |title=Mapping the locus of atrophia areata, a helicoid peripapillary chorioretinal degeneration with autosomal dominant inheritance, to chromosome 11p15. |journal=Hum. Mol. Genet. |volume=4 |issue= 3 |pages= 479-83 |year= 1995 |pmid= 7795606 |doi=  }}
*{{cite journal  | author=Kariya K, Farrance IK, Simpson PC |title=Transcriptional enhancer factor-1 in cardiac myocytes interacts with an alpha 1-adrenergic- and beta-protein kinase C-inducible element in the rat beta-myosin heavy chain promoter. |journal=J. Biol. Chem. |volume=268 |issue= 35 |pages= 26658-62 |year= 1994 |pmid= 8253797 |doi=  }}
*{{cite journal | author=Shimizu N, Smith G, Izumo S |title=Both a ubiquitous factor mTEF-1 and a distinct muscle-specific factor bind to the M-CAT motif of the myosin heavy chain beta gene. |journal=Nucleic Acids Res. |volume=21 |issue= 17 |pages= 4103-10 |year= 1993 |pmid= 8396764 |doi=  }}
*{{cite journal  | author=Stewart AF, Richard CW, Suzow J, ''et al.'' |title=Cloning of human RTEF-1, a transcriptional enhancer factor-1-related gene preferentially expressed in skeletal muscle: evidence for an ancient multigene family. |journal=Genomics |volume=37 |issue= 1 |pages= 68-76 |year= 1997 |pmid= 8921372 |doi=  }}
*{{cite journal  | author=Gupta MP, Amin CS, Gupta M, ''et al.'' |title=Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression. |journal=Mol. Cell. Biol. |volume=17 |issue= 7 |pages= 3924-36 |year= 1997 |pmid= 9199327 |doi=  }}
*{{cite journal  | author=Simmonds AJ, Liu X, Soanes KH, ''et al.'' |title=Molecular interactions between Vestigial and Scalloped promote wing formation in Drosophila. |journal=Genes Dev. |volume=12 |issue= 24 |pages= 3815-20 |year= 1999 |pmid= 9869635 |doi=  }}
*{{cite journal  | author=Jacquemin P, Depetris D, Mattei MG, ''et al.'' |title=Localization of human transcription factor TEF-4 and TEF-5 (TEAD2, TEAD3) genes to chromosomes 19q13.3 and 6p21.2 using fluorescence in situ hybridization and radiation hybrid analysis. |journal=Genomics |volume=55 |issue= 1 |pages= 127-9 |year= 1999 |pmid= 9889009 |doi= 10.1006/geno.1998.5628 }}
*{{cite journal | author=Vaudin P, Delanoue R, Davidson I, ''et al.'' |title=TONDU (TDU), a novel human protein related to the product of vestigial (vg) gene of Drosophila melanogaster interacts with vertebrate TEF factors and substitutes for Vg function in wing formation. |journal=Development |volume=126 |issue= 21 |pages= 4807-16 |year= 1999 |pmid= 10518497 |doi=  }}
*{{cite journal  | author=Gupta M, Kogut P, Davis FJ, ''et al.'' |title=Physical interaction between the MADS box of serum response factor and the TEA/ATTS DNA-binding domain of transcription enhancer factor-1. |journal=J. Biol. Chem. |volume=276 |issue= 13 |pages= 10413-22 |year= 2001 |pmid= 11136726 |doi= 10.1074/jbc.M008625200 }}
*{{cite journal  | author=Vassilev A, Kaneko KJ, Shu H, ''et al.'' |title=TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm. |journal=Genes Dev. |volume=15 |issue= 10 |pages= 1229-41 |year= 2001 |pmid= 11358867 |doi= 10.1101/gad.888601 }}
*{{cite journal  | author=Carlini LE, Getz MJ, Strauch AR, Kelm RJ |title=Cryptic MCAT enhancer regulation in fibroblasts and smooth muscle cells. Suppression of TEF-1 mediated activation by the single-stranded DNA-binding proteins, Pur alpha, Pur beta, and MSY1. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8682-92 |year= 2002 |pmid= 11751932 |doi= 10.1074/jbc.M109754200 }}
*{{cite journal  | author=Maeda T, Gupta MP, Stewart AF |title=TEF-1 and MEF2 transcription factors interact to regulate muscle-specific promoters. |journal=Biochem. Biophys. Res. Commun. |volume=294 |issue= 4 |pages= 791-7 |year= 2002 |pmid= 12061776 |doi= 10.1016/S0006-291X(02)00556-9 }}
*{{cite journal  | author=Maeda T, Chapman DL, Stewart AF |title=Mammalian vestigial-like 2, a cofactor of TEF-1 and MEF2 transcription factors that promotes skeletal muscle differentiation. |journal=J. Biol. Chem. |volume=277 |issue= 50 |pages= 48889-98 |year= 2003 |pmid= 12376544 |doi= 10.1074/jbc.M206858200 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Thompson M, Andrade VA, Andrade SJ, ''et al.'' |title=Inhibition of the TEF/TEAD transcription factor activity by nuclear calcium and distinct kinase pathways. |journal=Biochem. Biophys. Res. Commun. |volume=301 |issue= 2 |pages= 267-74 |year= 2003 |pmid= 12565854 |doi=  }}
*{{cite journal  | author=Karasseva N, Tsika G, Ji J, ''et al.'' |title=Transcription enhancer factor 1 binds multiple muscle MEF2 and A/T-rich elements during fast-to-slow skeletal muscle fiber type transitions. |journal=Mol. Cell. Biol. |volume=23 |issue= 15 |pages= 5143-64 |year= 2003 |pmid= 12861002 |doi=  }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Günther S, Mielcarek M, Krüger M, Braun T |title=VITO-1 is an essential cofactor of TEF1-dependent muscle-specific gene regulation. |journal=Nucleic Acids Res. |volume=32 |issue= 2 |pages= 791-802 |year= 2004 |pmid= 14762206 |doi= 10.1093/nar/gkh248 }}
}}
{{refend}}


{{protein-stub}}
Another conserved domain of TEAD1 is located at the C terminus of the protein. It allows the binding of cofactors and has been called the YAP1 binding domain, because it is its ability to bind this well-known TEAD proteins co-factor that led to its identification. Indeed, TEAD proteins cannot induce gene expression on their own. They have to associate with cofactors to be able to act<ref>{{cite journal | vauthors = Azakie A, Lamont L, Fineman JR, He Y | title = Divergent transcriptional enhancer factor-1 regulates the cardiac troponin T promoter | journal = American Journal of Physiology. Cell Physiology | volume = 289 | issue = 6 | pages = C1522–34 | date = December 2005 | pmid = 16049055 | doi = 10.1152/ajpcell.00126.2005 }}</ref>
{{Transcription factors}}
 
{{WikiDoc Sources}}
== Tissue distribution  ==
 
TEAD1 is expressed in various tissues including skeletal muscle, pancreas, placenta, lung, and heart.<ref name="ReferenceB">{{cite journal | vauthors = Xiao JH, Davidson I, Matthes H, Garnier JM, Chambon P | title = Cloning, expression, and transcriptional properties of the human enhancer factor TEF-1 | journal = Cell | volume = 65 | issue = 4 | pages = 551–68 | date = May 1991 | pmid = 1851669 | doi=10.1016/0092-8674(91)90088-g}}</ref><ref>{{cite journal | vauthors = Jacquemin P, Hwang JJ, Martial JA, Dollé P, Davidson I | title = A novel family of developmentally regulated mammalian transcription factors containing the TEA/ATTS DNA binding domain | journal = The Journal of Biological Chemistry | volume = 271 | issue = 36 | pages = 21775–85 | date = September 1996 | pmid = 8702974 | doi=10.1074/jbc.271.36.21775}}</ref><ref>{{cite journal | vauthors = Stewart AF, Richard CW, Suzow J, Stephan D, Weremowicz S, Morton CC, Adra CN | title = Cloning of human RTEF-1, a transcriptional enhancer factor-1-related gene preferentially expressed in skeletal muscle: evidence for an ancient multigene family | journal = Genomics | volume = 37 | issue = 1 | pages = 68–76 | date = October 1996 | pmid = 8921372 | doi=10.1006/geno.1996.0522}}</ref><ref>{{cite journal | vauthors = Yasunami M, Suzuki K, Houtani T, Sugimoto T, Ohkubo H | title = Molecular characterization of cDNA encoding a novel protein related to transcriptional enhancer factor-1 from neural precursor cells | journal = The Journal of Biological Chemistry | volume = 270 | issue = 31 | pages = 18649–54 | date = August 1995 | pmid = 7629195 | doi=10.1074/jbc.270.31.18649}}</ref><ref>{{cite journal | vauthors = Yasunami M, Suzuki K, Ohkubo H | title = A novel family of TEA domain-containing transcription factors with distinct spatiotemporal expression patterns | journal = Biochemical and Biophysical Research Communications | volume = 228 | issue = 2 | pages = 365–70 | date = November 1996 | pmid = 8920920 | doi = 10.1006/bbrc.1996.1667 }}</ref><ref>{{cite journal | vauthors = Yockey CE, Smith G, Izumo S, Shimizu N | title = cDNA cloning and characterization of murine transcriptional enhancer factor-1-related protein 1, a transcription factor that binds to the M-CAT motif | journal = The Journal of Biological Chemistry | volume = 271 | issue = 7 | pages = 3727–36 | date = February 1996 | pmid = 8631987 }}</ref><ref>{{cite journal | vauthors = Azakie A, Lamont L, Fineman JR, He Y | title = Divergent transcriptional enhancer factor-1 regulates the cardiac troponin T promoter | journal = American Journal of Physiology. Cell Physiology | volume = 289 | issue = 6 | pages = C1522-34 | date = December 2005 | pmid = 16049055 | doi = 10.1152/ajpcell.00126.2005 }}</ref>
 
== Orthologs  ==
 
TEAD proteins are found in many organisms under different names, assuming different functions.  For example, in Saccharomyces cerevisiae TEC-1 regulates the transposable element TY1 and is involved in pseudohyphale growth (the elongated shape that yeasts take when grown in nutrient-poor conditions).<ref>{{cite journal | vauthors = Laloux I, Dubois E, Dewerchin M, Jacobs E | title = TEC1, a gene involved in the activation of Ty1 and Ty1-mediated gene expression in Saccharomyces cerevisiae: cloning and molecular analysis | journal = Molecular and Cellular Biology | volume = 10 | issue = 7 | pages = 3541–50 | date = July 1990 | pmid = 2192259 | doi=10.1128/mcb.10.7.3541 | pmc=360789}}</ref> In Aspergillus nidulans, the TEA domain protein ABAA regulates the differentiation of conidiophores.<ref>{{cite journal | vauthors = Boylan MT, Mirabito PM, Willett CE, Zimmerman CR, Timberlake WE | title = Isolation and physical characterization of three essential conidiation genes from Aspergillus nidulans | journal = Molecular and Cellular Biology | volume = 7 | issue = 9 | pages = 3113–8 | date = September 1987 | pmid = 2823119 | doi=10.1128/mcb.7.9.3113 | pmc=367944}}</ref> In drosophila the transcription factor Scalloped is involved in the development of the wing disc, survival and cell growth.<ref>{{cite journal | vauthors = Goulev Y, Fauny JD, Gonzalez-Marti B, Flagiello D, Silber J, Zider A | title = SCALLOPED interacts with YORKIE, the nuclear effector of the hippo tumor-suppressor pathway in Drosophila | journal = Current Biology | volume = 18 | issue = 6 | pages = 435–41 | date = March 2008 | pmid = 18313299 | doi = 10.1016/j.cub.2008.02.034 }}</ref> Finally in Xenopus it has been demonstrated that the ortholog of TEAD1 regulates muscle differentiation.<ref>{{cite journal | vauthors = Naye F, Tréguer K, Soulet F, Faucheux C, Fédou S, Thézé N, Thiébaud P | title = Differential expression of two TEF-1 (TEAD) genes during Xenopus laevis development and in response to inducing factors | journal = The International Journal of Developmental Biology | volume = 51 | issue = 8 | pages = 745–52 | date = 2007 | pmid = 17939122 | doi = 10.1387/ijdb.072375fn }}</ref>
 
== Function ==
 
* Heart development (myocardium differentiation,<ref>{{cite journal | vauthors = Chen Z, Friedrich GA, Soriano P | title = Transcriptional enhancer factor 1 disruption by a retroviral gene trap leads to heart defects and embryonic lethality in mice | journal = Genes & Development | volume = 8 | issue = 19 | pages = 2293–301 | date = October 1994 | pmid = 7958896 | doi=10.1101/gad.8.19.2293}}</ref>
* Skeletal muscle development (alpha-actin of skeletal muscles),<ref name="ReferenceC">{{cite journal | vauthors = Jiang SW, Trujillo MA, Sakagashira M, Wilke RA, Eberhardt NL | title = Novel human TEF-1 isoforms exhibit altered DNA binding and functional properties | journal = Biochemistry | volume = 39 | issue = 12 | pages = 3505–13 | date = March 2000 | pmid = 10727247 | doi=10.1021/bi991048w}}</ref><ref>{{cite journal | vauthors = Karns LR, Kariya K, Simpson PC | title = M-CAT, CArG, and Sp1 elements are required for alpha 1-adrenergic induction of the skeletal alpha-actin promoter during cardiac myocyte hypertrophy. Transcriptional enhancer factor-1 and protein kinase C as conserved transducers of the fetal program in cardiac growth | journal = The Journal of Biological Chemistry | volume = 270 | issue = 1 | pages = 410–7 | date = January 1995 | pmid = 7814403 | doi=10.1074/jbc.270.1.410}}</ref><ref>{{cite journal | vauthors = Benhaddou A, Keime C, Ye T, Morlon A, Michel I, Jost B, Mengus G, Davidson I | title = Transcription factor TEAD4 regulates expression of myogenin and the unfolded protein response genes during C2C12 cell differentiation | journal = Cell Death and Differentiation | volume = 19 | issue = 2 | pages = 220–31 | date = February 2012 | pmid = 21701496 | doi = 10.1038/cdd.2011.87 | pmc=3263497}}</ref>)
* Smooth muscle development (alpha-actin of smooth muscles),<ref name="ReferenceC"/><ref>{{cite journal | vauthors = Swartz EA, Johnson AD, Owens GK | title = Two MCAT elements of the SM alpha-actin promoter function differentially in SM vs. non-SM cells | journal = The American Journal of Physiology | volume = 275 | issue = 2 Pt 1 | pages = C608-18 | date = August 1998 | pmid = 9688616 }}</ref>
* Regulation of myosin heavy chain genes,<ref>{{cite journal | vauthors = Rindt H, Gulick J, Knotts S, Neumann J, Robbins J | title = In vivo analysis of the murine beta-myosin heavy chain gene promoter | journal = The Journal of Biological Chemistry | volume = 268 | issue = 7 | pages = 5332–8 | date = March 1993 | pmid = 8444907 }}</ref> cardiac muscular genes troponin T and I <ref name="ReferenceA"/>
* Regulation of proliferation,<ref name="Zhao B 2015">{{cite journal | vauthors = Yu FX, Zhao B, Guan KL | title = Hippo Pathway in Organ Size Control, Tissue Homeostasis, and Cancer | journal = Cell | volume = 163 | issue = 4 | pages = 811–28 | date = November 2015 | pmid = 26544935 | doi = 10.1016/j.cell.2015.10.044 }}</ref><ref>{{cite journal | vauthors = Landin Malt A, Cagliero J, Legent K, Silber J, Zider A, Flagiello D | title = Alteration of TEAD1 expression levels confers apoptotic resistance through the transcriptional up-regulation of Livin | journal = PLoS One | volume = 7 | issue = 9 | pages = e45498 | date = 2012 | pmid = 23029054 | doi = 10.1371/journal.pone.0045498 | pmc=3454436}}</ref><ref>{{cite journal | vauthors = Zhao B, Li L, Lei Q, Guan KL | title = The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version | journal = Genes & Development | volume = 24 | issue = 9 | pages = 862–74 | date = May 2010 | pmid = 20439427 | doi = 10.1101/gad.1909210 | pmc=2861185}}</ref>
* Regulation of apoptosis,<ref>{{cite journal | vauthors = Landin Malt A, Cagliero J, Legent K, Silber J, Zider A, Flagiello D | title = Alteration of TEAD1 expression levels confers apoptotic resistance through the transcriptional up-regulation of Livin | journal = PLoS One | volume = 7 | issue = 9 | pages = e45498 | date = 2012 | pmid = 23029054 | doi = 10.1371/journal.pone.0045498 | pmc=3454436}}</ref><ref name="Landin Malt A 2013">{{cite journal | vauthors = Landin Malt A, Georges A, Silber J, Zider A, Flagiello D | title = Interaction with the Yes-associated protein (YAP) allows TEAD1 to positively regulate NAIP expression | journal = FEBS Letters | volume = 587 | issue = 19 | pages = 3216–23 | date = October 2013 | pmid = 23994529 | doi = 10.1016/j.febslet.2013.08.013 }}</ref>
 
== Post-transcriptional modifications  ==
 
Protein Kinase A (pKA) can phosphorylate TEAD1 at serine 102, after the TEA domain. This phosphorylation is needed for the transcriptional activation of the α MyHC gene.<ref>{{cite journal | vauthors = Gupta MP, Gupta M, Dizon E, Zak R | title = Sympathetic control of cardiac myosin heavy chain gene expression | journal = Molecular and Cellular Biochemistry | volume = 157 | issue = 1–2 | pages = 117–24 | date = 1996 | pmid = 8739237 | doi=10.1007/bf00227889}}</ref> Protein Kinase C (pKC) phosphorylates TEAD1 on serine and threonine next to the last alpha loop in the TEA domain. This phosphorylation decreases TEAD1 binding to the GTIIC enhancer.<ref>{{cite journal | vauthors = Jiang SW, Dong M, Trujillo MA, Miller LJ, Eberhardt NL | title = DNA binding of TEA/ATTS domain factors is regulated by protein kinase C phosphorylation in human choriocarcinoma cells | journal = The Journal of Biological Chemistry | volume = 276 | issue = 26 | pages = 23464–70 | date = June 2001 | pmid = 11313339 | doi = 10.1074/jbc.M010934200 }}</ref>
TEAD1 can be palmitoylated on a conserved cysteine at the C-term of the protein. This post-translational modification is critical for proper folding of TEAD proteins and their stability.<ref>{{cite journal | vauthors = Noland CL, Gierke S, Schnier PD, Murray J, Sandoval WN, Sagolla M, Dey A, Hannoush RN, Fairbrother WJ, Cunningham CN | title = Palmitoylation of TEAD Transcription Factors Is Required for Their Stability and Function in Hippo Pathway Signaling | journal = Structure | volume = 24 | issue = 1 | pages = 179–86 | date = January 2016 | pmid = 26724994 | doi = 10.1016/j.str.2015.11.005 }}</ref>
 
== Cofactors ==
 
TEAD proteins require cofactors to induce the transcription of target genes.<ref name="ReferenceB"/> TEAD1 interacts with all members of the SRC family of steroid receptor coactivators. In HeLa cells TEAD1 and SRC induce gene expression,<ref>{{cite journal | vauthors = Belandia B, Parker MG | title = Functional interaction between the p160 coactivator proteins and the transcriptional enhancer factor family of transcription factors | journal = The Journal of Biological Chemistry | volume = 275 | issue = 40 | pages = 30801–5 | date = October 2000 | pmid = 10934189 | doi = 10.1074/jbc.C000484200 }}</ref> TEAD1 interacts with PARP (Poly-ADP ribose polymerase) to regulate smooth muscle α-actin expression. PARP can also ADP-ribosylate the TEAD proteins and make the chromatin context favorable to transcription through histone modification,<ref>{{cite journal | vauthors = Butler AJ, Ordahl CP | title = Poly(ADP-ribose) polymerase binds with transcription enhancer factor 1 to MCAT1 elements to regulate muscle-specific transcription | journal = Molecular and Cellular Biology | volume = 19 | issue = 1 | pages = 296–306 | date = January 1999 | pmid = 9858553 | doi=10.1128/mcb.19.1.296 | pmc=83887}}</ref> SRF (Serum response factor) and TEAD1 together regulate gene expression.<ref>{{cite journal | vauthors = MacLellan WR, Lee TC, Schwartz RJ, Schneider MD | title = Transforming growth factor-beta response elements of the skeletal alpha-actin gene. Combinatorial action of serum response factor, YY1, and the SV40 enhancer-binding protein, TEF-1 | journal = The Journal of Biological Chemistry | volume = 269 | issue = 24 | pages = 16754–60 | date = June 1994 | pmid = 8206998 }}</ref>
 
TEAD proteins and MEF2 (myocyte enhancer factor 2) interact physically. The binding of MEF2 on DNA induces and potentiates TEAD1 recruitment at MCAT sequences that are adjacent to MEF2 binding sites. This recruitment leads to the repression of the MLC2v (Myosin Light Chain 2 v) and βMHC ( β-myosin heavy chain ) promoter.<ref>{{cite journal | vauthors = Maeda T, Chapman DL, Stewart AF | title = Mammalian vestigial-like 2, a cofactor of TEF-1 and MEF2 transcription factors that promotes skeletal muscle differentiation | journal = The Journal of Biological Chemistry | volume = 277 | issue = 50 | pages = 48889–98 | date = December 2002 | pmid = 12376544 | doi = 10.1074/jbc.M206858200 }}</ref> TEAD1 and the phosphoprotein MAX interact in vivo and in vitro. Once this complex is formed, these two proteins can regulate the alpha-myosin heavy chain (α-MHC) gene expression.<ref>{{cite journal | vauthors = Gupta MP, Amin CS, Gupta M, Hay N, Zak R | title = Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression | journal = Molecular and Cellular Biology | volume = 17 | issue = 7 | pages = 3924–36 | date = July 1997 | pmid = 9199327 | doi=10.1128/mcb.17.7.3924 | pmc=232245}}</ref>
 
The four Vestigial-like (VGLL) proteins are able to interact with all TEADs.<ref>{{cite journal | vauthors = Chen L, Chan SW, Zhang X, Walsh M, Lim CJ, Hong W, Song H | title = Structural basis of YAP recognition by TEAD4 in the hippo pathway | journal = Genes & Development | volume = 24 | issue = 3 | pages = 290–300 | date = February 2010 | pmid = 20123908 | doi = 10.1101/gad.1865310 | pmc=2811830}}</ref> The precise function of TEAD and VGLL interaction is still poorly understood. It has been shown that TEAD/VGLL1 complexes promote anchorage-independent cell proliferation in prostate cancer cell lines suggesting a role in cancer progression <ref>{{cite journal | vauthors = Pobbati AV, Chan SW, Lee I, Song H, Hong W | title = Structural and functional similarity between the Vgll1-TEAD and the YAP-TEAD complexes | journal = Structure | volume = 20 | issue = 7 | pages = 1135–40 | date = July 2012 | pmid = 22632831 | doi = 10.1016/j.str.2012.04.004 }}</ref> Moreover, VGLL2 interaction with TEAD1 activates muscle promoter upon C2C12 differentiation and enhances MyoD-mediated myogenic in 10T1/2.<ref>{{cite journal | vauthors = Günther S, Mielcarek M, Krüger M, Braun T | title = VITO-1 is an essential cofactor of TEF1-dependent muscle-specific gene regulation | journal = Nucleic Acids Research | volume = 32 | issue = 2 | pages = 791–802 | date = 2004 | pmid = 14762206 | doi = 10.1093/nar/gkh248 | pmc=373362}}</ref> Finally the complex TEAD/VGLL4 acts as a default transcriptional repressor.<ref name="Koontz LM 2013">{{cite journal | vauthors = Koontz LM, Liu-Chittenden Y, Yin F, Zheng Y, Yu J, Huang B, Chen Q, Wu S, Pan D | title = The Hippo effector Yorkie controls normal tissue growth by antagonizing scalloped-mediated default repression | journal = Developmental Cell | volume = 25 | issue = 4 | pages = 388–401 | date = May 2013 | pmid = 23725764 | doi = 10.1016/j.devcel.2013.04.021 | pmc=3705890}}</ref>
 
The interaction between YAP (Yes Associated Protein 65), TAZ, a transcriptional coactivator paralog to YAP, and all TEAD proteins was demonstrated both in vitro and in vivo. In both cases the interaction of the proteins leads to increased TEAD transcriptional activity.<ref name="Koontz LM 2013"/><ref>{{cite journal | vauthors = Vassilev A, Kaneko KJ, Shu H, Zhao Y, DePamphilis ML | title = TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm | journal = Genes & Development | volume = 15 | issue = 10 | pages = 1229–41 | date = May 2001 | pmid = 11358867 | doi = 10.1101/gad.888601 | pmc=313800}}</ref> YAP/TAZ are effectors of the Hippo tumor suppressor pathway that restricts organ growth by keeping in check cell proliferation and promoting apoptosis in mammals and also in Drosophila.<ref name="Zhao B 2015"/><ref>{{cite journal | vauthors = Zhao B, Li L, Lei Q, Guan KL | title = The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version | journal = Genes & Development | volume = 24 | issue = 9 | pages = 862–74 | date = May 2010 | pmid = 20439427 | doi = 10.1101/gad.1909210 | pmc=2861185}}</ref>
 
== Role in cancer ==
 
Analysis of cancer transcriptome databases (www.ebi.ac.uk/gxa) showed that TEAD1 is dysregulated in several types of cancers. First in Kaposi sarcoma there is a 300-fold increase in TEAD1 levels. Moreover, the increase of TEAD expression can be detected in basal-like breast cancers,<ref>{{cite journal | vauthors = Han W, Jung EM, Cho J, Lee JW, Hwang KT, Yang SJ, Kang JJ, Bae JY, Jeon YK, Park IA, Nicolau M, Jeffrey SS, Noh DY | title = DNA copy number alterations and expression of relevant genes in triple-negative breast cancer | journal = Genes, Chromosomes & Cancer | volume = 47 | issue = 6 | pages = 490–9 | date = June 2008 | pmid = 18314908 | doi = 10.1002/gcc.20550 }}</ref><ref>{{cite journal | vauthors = Richardson AL, Wang ZC, De Nicolo A, Lu X, Brown M, Miron A, Liao X, Iglehart JD, Livingston DM, Ganesan S | title = X chromosomal abnormalities in basal-like human breast cancer | journal = Cancer Cell | volume = 9 | issue = 2 | pages = 121–32 | date = February 2006 | pmid = 16473279 | doi = 10.1016/j.ccr.2006.01.013 }}</ref> fallopian tube carcinoma,<ref>{{cite journal | vauthors = Nowee ME, Snijders AM, Rockx DA, de Wit RM, Kosma VM, Hämäläinen K, Schouten JP, Verheijen RH, van Diest PJ, Albertson DG, Dorsman JC | title = DNA profiling of primary serous ovarian and fallopian tube carcinomas with array comparative genomic hybridization and multiplex ligation-dependent probe amplification | journal = The Journal of Pathology | volume = 213 | issue = 1 | pages = 46–55 | date = September 2007 | pmid = 17668415 | doi = 10.1002/path.2217 }}</ref> and germ cell tumors.<ref>{{cite journal | vauthors = Skotheim RI, Autio R, Lind GE, Kraggerud SM, Andrews PW, Monni O, Kallioniemi O, Lothe RA | title = Novel genomic aberrations in testicular germ cell tumors by array-CGH, and associated gene expression changes | journal = Cellular Oncology | volume = 28 | issue = 5-6 | pages = 315–26 | date = 2006 | pmid = 17167184 | pmc=4615958}}</ref> Otherwise, in other types of cancer TEAD expression is decreased, for example in other breast cancer types and in renal or bladder cancers. This dual role can be explained by the different targets and the differential regulation of target genes by TEAD transcription factors.<ref name="Landin Malt A 2013"/><ref>{{cite journal | vauthors = Landin Malt A, Cagliero J, Legent K, Silber J, Zider A, Flagiello D | title = Alteration of TEAD1 expression levels confers apoptotic resistance through the transcriptional up-regulation of Livin | journal = PLoS One | volume = 7 | issue = 9 | pages = e45498 | date = 2012 | pmid = 23029054 | doi = 10.1371/journal.pone.0045498 | pmc=3454436}}</ref> Finally recent studies showed that TEAD1 and YAP in ovarian cancer can induces cell stemness and chemoresistance.<ref>{{cite journal | vauthors = Xia Y, Zhang YL, Yu C, Chang T, Fan HY | title = YAP/TEAD co-activator regulated pluripotency and chemoresistance in ovarian cancer initiated cells | journal = PLoS One | volume = 9 | issue = 11 | pages = e109575 | date = 2014 | pmid = 25369529 | doi = 10.1371/journal.pone.0109575 | pmc=4219672}}</ref> and that genetic variant of TEAD protein and YAP are enriched in some cancers.<ref>{{cite journal | vauthors = Yuan H, Liu H, Liu Z, Zhu D, Amos CI, Fang S, Lee JE, Wei Q | title = Genetic variants in Hippo pathway genes YAP1, TEAD1 and TEAD4 are associated with melanoma-specific survival | journal = International Journal of Cancer | volume = 137 | issue = 3 | pages = 638–45 | date = August 2015 | pmid = 25628125 | doi = 10.1002/ijc.29429 | pmc = 4437894 }}</ref>
 
== References ==
{{Reflist|33em}}
 
== Further reading ==
{{Refbegin|33em}}
* {{cite journal | vauthors = Boam DS, Davidson I, Chambon P | title = A TATA-less promoter containing binding sites for ubiquitous transcription factors mediates cell type-specific regulation of the gene for transcription enhancer factor-1 (TEF-1) | journal = The Journal of Biological Chemistry | volume = 270 | issue = 33 | pages = 19487–94 | date = August 1995 | pmid = 7642633 | doi = 10.1074/jbc.270.33.19487 }}
* {{cite journal | vauthors = Fossdal R, Magnússon L, Weber JL, Jensson O | title = Mapping the locus of atrophia areata, a helicoid peripapillary chorioretinal degeneration with autosomal dominant inheritance, to chromosome 11p15 | journal = Human Molecular Genetics | volume = 4 | issue = 3 | pages = 479–83 | date = March 1995 | pmid = 7795606 | doi = 10.1093/hmg/4.3.479 }}
* {{cite journal | vauthors = Kariya K, Farrance IK, Simpson PC | title = Transcriptional enhancer factor-1 in cardiac myocytes interacts with an alpha 1-adrenergic- and beta-protein kinase C-inducible element in the rat beta-myosin heavy chain promoter | journal = The Journal of Biological Chemistry | volume = 268 | issue = 35 | pages = 26658–62 | date = December 1993 | pmid = 8253797 | doi =  }}
* {{cite journal | vauthors = Shimizu N, Smith G, Izumo S | title = Both a ubiquitous factor mTEF-1 and a distinct muscle-specific factor bind to the M-CAT motif of the myosin heavy chain beta gene | journal = Nucleic Acids Research | volume = 21 | issue = 17 | pages = 4103–10 | date = August 1993 | pmid = 8396764 | pmc = 310013 | doi = 10.1093/nar/21.17.4103 }}
* {{cite journal | vauthors = Stewart AF, Richard CW, Suzow J, Stephan D, Weremowicz S, Morton CC, Adra CN | title = Cloning of human RTEF-1, a transcriptional enhancer factor-1-related gene preferentially expressed in skeletal muscle: evidence for an ancient multigene family | journal = Genomics | volume = 37 | issue = 1 | pages = 68–76 | date = October 1996 | pmid = 8921372 | doi = 10.1006/geno.1996.0522 }}
* {{cite journal | vauthors = Gupta MP, Amin CS, Gupta M, Hay N, Zak R | title = Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression | journal = Molecular and Cellular Biology | volume = 17 | issue = 7 | pages = 3924–36 | date = July 1997 | pmid = 9199327 | pmc = 232245 | doi = 10.1128/mcb.17.7.3924 }}
* {{cite journal | vauthors = Simmonds AJ, Liu X, Soanes KH, Krause HM, Irvine KD, Bell JB | title = Molecular interactions between Vestigial and Scalloped promote wing formation in Drosophila | journal = Genes & Development | volume = 12 | issue = 24 | pages = 3815–20 | date = December 1998 | pmid = 9869635 | pmc = 317270 | doi = 10.1101/gad.12.24.3815 }}
* {{cite journal | vauthors = Vaudin P, Delanoue R, Davidson I, Silber J, Zider A | title = TONDU (TDU), a novel human protein related to the product of vestigial (vg) gene of Drosophila melanogaster interacts with vertebrate TEF factors and substitutes for Vg function in wing formation | journal = Development | volume = 126 | issue = 21 | pages = 4807–16 | date = November 1999 | pmid = 10518497 | doi =  }}
* {{cite journal | vauthors = Gupta M, Kogut P, Davis FJ, Belaguli NS, Schwartz RJ, Gupta MP | title = Physical interaction between the MADS box of serum response factor and the TEA/ATTS DNA-binding domain of transcription enhancer factor-1 | journal = The Journal of Biological Chemistry | volume = 276 | issue = 13 | pages = 10413–22 | date = March 2001 | pmid = 11136726 | doi = 10.1074/jbc.M008625200 }}
* {{cite journal | vauthors = Vassilev A, Kaneko KJ, Shu H, Zhao Y, DePamphilis ML | title = TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm | journal = Genes & Development | volume = 15 | issue = 10 | pages = 1229–41 | date = May 2001 | pmid = 11358867 | pmc = 313800 | doi = 10.1101/gad.888601 }}
* {{cite journal | vauthors = Carlini LE, Getz MJ, Strauch AR, Kelm RJ | title = Cryptic MCAT enhancer regulation in fibroblasts and smooth muscle cells. Suppression of TEF-1 mediated activation by the single-stranded DNA-binding proteins, Pur alpha, Pur beta, and MSY1 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 10 | pages = 8682–92 | date = March 2002 | pmid = 11751932 | doi = 10.1074/jbc.M109754200 }}
* {{cite journal | vauthors = Maeda T, Gupta MP, Stewart AF | title = TEF-1 and MEF2 transcription factors interact to regulate muscle-specific promoters | journal = Biochemical and Biophysical Research Communications | volume = 294 | issue = 4 | pages = 791–7 | date = June 2002 | pmid = 12061776 | doi = 10.1016/S0006-291X(02)00556-9 }}
* {{cite journal | vauthors = Maeda T, Chapman DL, Stewart AF | title = Mammalian vestigial-like 2, a cofactor of TEF-1 and MEF2 transcription factors that promotes skeletal muscle differentiation | journal = The Journal of Biological Chemistry | volume = 277 | issue = 50 | pages = 48889–98 | date = December 2002 | pmid = 12376544 | doi = 10.1074/jbc.M206858200 }}
* {{cite journal | vauthors = Thompson M, Andrade VA, Andrade SJ, Pusl T, Ortega JM, Goes AM, Leite MF | title = Inhibition of the TEF/TEAD transcription factor activity by nuclear calcium and distinct kinase pathways | journal = Biochemical and Biophysical Research Communications | volume = 301 | issue = 2 | pages = 267–74 | date = February 2003 | pmid = 12565854 | doi = 10.1016/S0006-291X(02)03024-3 }}
* {{cite journal | vauthors = Karasseva N, Tsika G, Ji J, Zhang A, Mao X, Tsika R | title = Transcription enhancer factor 1 binds multiple muscle MEF2 and A/T-rich elements during fast-to-slow skeletal muscle fiber type transitions | journal = Molecular and Cellular Biology | volume = 23 | issue = 15 | pages = 5143–64 | date = August 2003 | pmid = 12861002 | pmc = 165722 | doi = 10.1128/MCB.23.15.5143-5164.2003 }}
* {{cite journal | vauthors = Günther S, Mielcarek M, Krüger M, Braun T | title = VITO-1 is an essential cofactor of TEF1-dependent muscle-specific gene regulation | journal = Nucleic Acids Research | volume = 32 | issue = 2 | pages = 791–802 | year = 2004 | pmid = 14762206 | pmc = 373362 | doi = 10.1093/nar/gkh248 }}
{{Refend}}
 
{{PDB Gallery|geneid=7003}}
{{Transcription factors|g3}}

Latest revision as of 21:07, 15 May 2018

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Transcriptional enhancer factor TEF-1 also known as TEA domain family member 1 (TEAD1) and transcription factor 13 (TCF-13) is a protein that in humans is encoded by the TEAD1 gene.[1][2][3][4] TEAD1 was the first member of the TEAD family of transcription factors to be identified.[1][5]

File:TEAD1Wiki figure.jpg

Structure

All members of the TEAD family share a highly conserved DNA binding domain called the TEA domain.[6] This DNA binding domain has a consensus DNA sequence 5’-CATTCCA/T-3’ that is called the MCAT element.[7] The three dimensional structure of the TEA domain has been identified [5]. Its conformation is close to that of the homeodomain and contains 3 α helixes (H1, H2 and H3). It is the H3 helix that enables TEAD proteins to bind DNA.[8]

Another conserved domain of TEAD1 is located at the C terminus of the protein. It allows the binding of cofactors and has been called the YAP1 binding domain, because it is its ability to bind this well-known TEAD proteins co-factor that led to its identification. Indeed, TEAD proteins cannot induce gene expression on their own. They have to associate with cofactors to be able to act[9]

Tissue distribution

TEAD1 is expressed in various tissues including skeletal muscle, pancreas, placenta, lung, and heart.[10][11][12][13][14][15][16]

Orthologs

TEAD proteins are found in many organisms under different names, assuming different functions. For example, in Saccharomyces cerevisiae TEC-1 regulates the transposable element TY1 and is involved in pseudohyphale growth (the elongated shape that yeasts take when grown in nutrient-poor conditions).[17] In Aspergillus nidulans, the TEA domain protein ABAA regulates the differentiation of conidiophores.[18] In drosophila the transcription factor Scalloped is involved in the development of the wing disc, survival and cell growth.[19] Finally in Xenopus it has been demonstrated that the ortholog of TEAD1 regulates muscle differentiation.[20]

Function

  • Heart development (myocardium differentiation,[21]
  • Skeletal muscle development (alpha-actin of skeletal muscles),[22][23][24])
  • Smooth muscle development (alpha-actin of smooth muscles),[22][25]
  • Regulation of myosin heavy chain genes,[26] cardiac muscular genes troponin T and I [5]
  • Regulation of proliferation,[27][28][29]
  • Regulation of apoptosis,[30][31]

Post-transcriptional modifications

Protein Kinase A (pKA) can phosphorylate TEAD1 at serine 102, after the TEA domain. This phosphorylation is needed for the transcriptional activation of the α MyHC gene.[32] Protein Kinase C (pKC) phosphorylates TEAD1 on serine and threonine next to the last alpha loop in the TEA domain. This phosphorylation decreases TEAD1 binding to the GTIIC enhancer.[33] TEAD1 can be palmitoylated on a conserved cysteine at the C-term of the protein. This post-translational modification is critical for proper folding of TEAD proteins and their stability.[34]

Cofactors

TEAD proteins require cofactors to induce the transcription of target genes.[10] TEAD1 interacts with all members of the SRC family of steroid receptor coactivators. In HeLa cells TEAD1 and SRC induce gene expression,[35] TEAD1 interacts with PARP (Poly-ADP ribose polymerase) to regulate smooth muscle α-actin expression. PARP can also ADP-ribosylate the TEAD proteins and make the chromatin context favorable to transcription through histone modification,[36] SRF (Serum response factor) and TEAD1 together regulate gene expression.[37]

TEAD proteins and MEF2 (myocyte enhancer factor 2) interact physically. The binding of MEF2 on DNA induces and potentiates TEAD1 recruitment at MCAT sequences that are adjacent to MEF2 binding sites. This recruitment leads to the repression of the MLC2v (Myosin Light Chain 2 v) and βMHC ( β-myosin heavy chain ) promoter.[38] TEAD1 and the phosphoprotein MAX interact in vivo and in vitro. Once this complex is formed, these two proteins can regulate the alpha-myosin heavy chain (α-MHC) gene expression.[39]

The four Vestigial-like (VGLL) proteins are able to interact with all TEADs.[40] The precise function of TEAD and VGLL interaction is still poorly understood. It has been shown that TEAD/VGLL1 complexes promote anchorage-independent cell proliferation in prostate cancer cell lines suggesting a role in cancer progression [41] Moreover, VGLL2 interaction with TEAD1 activates muscle promoter upon C2C12 differentiation and enhances MyoD-mediated myogenic in 10T1/2.[42] Finally the complex TEAD/VGLL4 acts as a default transcriptional repressor.[43]

The interaction between YAP (Yes Associated Protein 65), TAZ, a transcriptional coactivator paralog to YAP, and all TEAD proteins was demonstrated both in vitro and in vivo. In both cases the interaction of the proteins leads to increased TEAD transcriptional activity.[43][44] YAP/TAZ are effectors of the Hippo tumor suppressor pathway that restricts organ growth by keeping in check cell proliferation and promoting apoptosis in mammals and also in Drosophila.[27][45]

Role in cancer

Analysis of cancer transcriptome databases (www.ebi.ac.uk/gxa) showed that TEAD1 is dysregulated in several types of cancers. First in Kaposi sarcoma there is a 300-fold increase in TEAD1 levels. Moreover, the increase of TEAD expression can be detected in basal-like breast cancers,[46][47] fallopian tube carcinoma,[48] and germ cell tumors.[49] Otherwise, in other types of cancer TEAD expression is decreased, for example in other breast cancer types and in renal or bladder cancers. This dual role can be explained by the different targets and the differential regulation of target genes by TEAD transcription factors.[31][50] Finally recent studies showed that TEAD1 and YAP in ovarian cancer can induces cell stemness and chemoresistance.[51] and that genetic variant of TEAD protein and YAP are enriched in some cancers.[52]

References

  1. ↑ 1.0 1.1 Xiao JH, Davidson I, Matthes H, Garnier JM, Chambon P (May 1991). "Cloning, expression, and transcriptional properties of the human enhancer factor TEF-1". Cell. 65 (4): 551–68. doi:10.1016/0092-8674(91)90088-G. PMID 1851669.
  2. ↑ Jacquemin P, Depetris D, Mattei MG, Martial JA, Davidson I (Jan 1999). "Localization of human transcription factor TEF-4 and TEF-5 (TEAD2, TEAD3) genes to chromosomes 19q13.3 and 6p21.2 using fluorescence in situ hybridization and radiation hybrid analysis". Genomics. 55 (1): 127–9. doi:10.1006/geno.1998.5628. PMID 9889009.
  3. ↑ Fossdal R, Jonasson F, Kristjansdottir GT, Kong A, Stefansson H, Gosh S, Gulcher JR, Stefansson K (May 2004). "A novel TEAD1 mutation is the causative allele in Sveinsson's chorioretinal atrophy (helicoid peripapillary chorioretinal degeneration)". Human Molecular Genetics. 13 (9): 975–81. doi:10.1093/hmg/ddh106. PMID 15016762.
  4. ↑ "Entrez Gene: TEAD1 TEA domain family member 1 (SV40 transcriptional enhancer factor)".
  5. ↑ 5.0 5.1 Mar JH, Ordahl CP (September 1988). "A conserved CATTCCT motif is required for skeletal muscle-specific activity of the cardiac troponin T gene promoter". Proceedings of the National Academy of Sciences of the United States of America. 85 (17): 6404–8. doi:10.1073/pnas.85.17.6404. PMC 281980. PMID 3413104.
  6. ↑ Hwang JJ, Chambon P, Davidson I (June 1993). "Characterization of the transcription activation function and the DNA binding domain of transcriptional enhancer factor-1". The EMBO Journal. 12 (6): 2337–48. PMC 413464. PMID 8389695.
  7. ↑ Farrance IK, Mar JH, Ordahl CP (August 1992). "M-CAT binding factor is related to the SV40 enhancer binding factor, TEF-1". The Journal of Biological Chemistry. 267 (24): 17234–40. PMID 1324927.
  8. ↑ Anbanandam A, Albarado DC, Nguyen CT, Halder G, Gao X, Veeraraghavan S (November 2006). "Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain". Proceedings of the National Academy of Sciences of the United States of America. 103 (46): 17225–30. doi:10.1073/pnas.0607171103. PMC 1859914. PMID 17085591.
  9. ↑ Azakie A, Lamont L, Fineman JR, He Y (December 2005). "Divergent transcriptional enhancer factor-1 regulates the cardiac troponin T promoter". American Journal of Physiology. Cell Physiology. 289 (6): C1522–34. doi:10.1152/ajpcell.00126.2005. PMID 16049055.
  10. ↑ 10.0 10.1 Xiao JH, Davidson I, Matthes H, Garnier JM, Chambon P (May 1991). "Cloning, expression, and transcriptional properties of the human enhancer factor TEF-1". Cell. 65 (4): 551–68. doi:10.1016/0092-8674(91)90088-g. PMID 1851669.
  11. ↑ Jacquemin P, Hwang JJ, Martial JA, Dollé P, Davidson I (September 1996). "A novel family of developmentally regulated mammalian transcription factors containing the TEA/ATTS DNA binding domain". The Journal of Biological Chemistry. 271 (36): 21775–85. doi:10.1074/jbc.271.36.21775. PMID 8702974.
  12. ↑ Stewart AF, Richard CW, Suzow J, Stephan D, Weremowicz S, Morton CC, Adra CN (October 1996). "Cloning of human RTEF-1, a transcriptional enhancer factor-1-related gene preferentially expressed in skeletal muscle: evidence for an ancient multigene family". Genomics. 37 (1): 68–76. doi:10.1006/geno.1996.0522. PMID 8921372.
  13. ↑ Yasunami M, Suzuki K, Houtani T, Sugimoto T, Ohkubo H (August 1995). "Molecular characterization of cDNA encoding a novel protein related to transcriptional enhancer factor-1 from neural precursor cells". The Journal of Biological Chemistry. 270 (31): 18649–54. doi:10.1074/jbc.270.31.18649. PMID 7629195.
  14. ↑ Yasunami M, Suzuki K, Ohkubo H (November 1996). "A novel family of TEA domain-containing transcription factors with distinct spatiotemporal expression patterns". Biochemical and Biophysical Research Communications. 228 (2): 365–70. doi:10.1006/bbrc.1996.1667. PMID 8920920.
  15. ↑ Yockey CE, Smith G, Izumo S, Shimizu N (February 1996). "cDNA cloning and characterization of murine transcriptional enhancer factor-1-related protein 1, a transcription factor that binds to the M-CAT motif". The Journal of Biological Chemistry. 271 (7): 3727–36. PMID 8631987.
  16. ↑ Azakie A, Lamont L, Fineman JR, He Y (December 2005). "Divergent transcriptional enhancer factor-1 regulates the cardiac troponin T promoter". American Journal of Physiology. Cell Physiology. 289 (6): C1522–34. doi:10.1152/ajpcell.00126.2005. PMID 16049055.
  17. ↑ Laloux I, Dubois E, Dewerchin M, Jacobs E (July 1990). "TEC1, a gene involved in the activation of Ty1 and Ty1-mediated gene expression in Saccharomyces cerevisiae: cloning and molecular analysis". Molecular and Cellular Biology. 10 (7): 3541–50. doi:10.1128/mcb.10.7.3541. PMC 360789. PMID 2192259.
  18. ↑ Boylan MT, Mirabito PM, Willett CE, Zimmerman CR, Timberlake WE (September 1987). "Isolation and physical characterization of three essential conidiation genes from Aspergillus nidulans". Molecular and Cellular Biology. 7 (9): 3113–8. doi:10.1128/mcb.7.9.3113. PMC 367944. PMID 2823119.
  19. ↑ Goulev Y, Fauny JD, Gonzalez-Marti B, Flagiello D, Silber J, Zider A (March 2008). "SCALLOPED interacts with YORKIE, the nuclear effector of the hippo tumor-suppressor pathway in Drosophila". Current Biology. 18 (6): 435–41. doi:10.1016/j.cub.2008.02.034. PMID 18313299.
  20. ↑ Naye F, Tréguer K, Soulet F, Faucheux C, Fédou S, Thézé N, Thiébaud P (2007). "Differential expression of two TEF-1 (TEAD) genes during Xenopus laevis development and in response to inducing factors". The International Journal of Developmental Biology. 51 (8): 745–52. doi:10.1387/ijdb.072375fn. PMID 17939122.
  21. ↑ Chen Z, Friedrich GA, Soriano P (October 1994). "Transcriptional enhancer factor 1 disruption by a retroviral gene trap leads to heart defects and embryonic lethality in mice". Genes & Development. 8 (19): 2293–301. doi:10.1101/gad.8.19.2293. PMID 7958896.
  22. ↑ 22.0 22.1 Jiang SW, Trujillo MA, Sakagashira M, Wilke RA, Eberhardt NL (March 2000). "Novel human TEF-1 isoforms exhibit altered DNA binding and functional properties". Biochemistry. 39 (12): 3505–13. doi:10.1021/bi991048w. PMID 10727247.
  23. ↑ Karns LR, Kariya K, Simpson PC (January 1995). "M-CAT, CArG, and Sp1 elements are required for alpha 1-adrenergic induction of the skeletal alpha-actin promoter during cardiac myocyte hypertrophy. Transcriptional enhancer factor-1 and protein kinase C as conserved transducers of the fetal program in cardiac growth". The Journal of Biological Chemistry. 270 (1): 410–7. doi:10.1074/jbc.270.1.410. PMID 7814403.
  24. ↑ Benhaddou A, Keime C, Ye T, Morlon A, Michel I, Jost B, Mengus G, Davidson I (February 2012). "Transcription factor TEAD4 regulates expression of myogenin and the unfolded protein response genes during C2C12 cell differentiation". Cell Death and Differentiation. 19 (2): 220–31. doi:10.1038/cdd.2011.87. PMC 3263497. PMID 21701496.
  25. ↑ Swartz EA, Johnson AD, Owens GK (August 1998). "Two MCAT elements of the SM alpha-actin promoter function differentially in SM vs. non-SM cells". The American Journal of Physiology. 275 (2 Pt 1): C608–18. PMID 9688616.
  26. ↑ Rindt H, Gulick J, Knotts S, Neumann J, Robbins J (March 1993). "In vivo analysis of the murine beta-myosin heavy chain gene promoter". The Journal of Biological Chemistry. 268 (7): 5332–8. PMID 8444907.
  27. ↑ 27.0 27.1 Yu FX, Zhao B, Guan KL (November 2015). "Hippo Pathway in Organ Size Control, Tissue Homeostasis, and Cancer". Cell. 163 (4): 811–28. doi:10.1016/j.cell.2015.10.044. PMID 26544935.
  28. ↑ Landin Malt A, Cagliero J, Legent K, Silber J, Zider A, Flagiello D (2012). "Alteration of TEAD1 expression levels confers apoptotic resistance through the transcriptional up-regulation of Livin". PLoS One. 7 (9): e45498. doi:10.1371/journal.pone.0045498. PMC 3454436. PMID 23029054.
  29. ↑ Zhao B, Li L, Lei Q, Guan KL (May 2010). "The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version". Genes & Development. 24 (9): 862–74. doi:10.1101/gad.1909210. PMC 2861185. PMID 20439427.
  30. ↑ Landin Malt A, Cagliero J, Legent K, Silber J, Zider A, Flagiello D (2012). "Alteration of TEAD1 expression levels confers apoptotic resistance through the transcriptional up-regulation of Livin". PLoS One. 7 (9): e45498. doi:10.1371/journal.pone.0045498. PMC 3454436. PMID 23029054.
  31. ↑ 31.0 31.1 Landin Malt A, Georges A, Silber J, Zider A, Flagiello D (October 2013). "Interaction with the Yes-associated protein (YAP) allows TEAD1 to positively regulate NAIP expression". FEBS Letters. 587 (19): 3216–23. doi:10.1016/j.febslet.2013.08.013. PMID 23994529.
  32. ↑ Gupta MP, Gupta M, Dizon E, Zak R (1996). "Sympathetic control of cardiac myosin heavy chain gene expression". Molecular and Cellular Biochemistry. 157 (1–2): 117–24. doi:10.1007/bf00227889. PMID 8739237.
  33. ↑ Jiang SW, Dong M, Trujillo MA, Miller LJ, Eberhardt NL (June 2001). "DNA binding of TEA/ATTS domain factors is regulated by protein kinase C phosphorylation in human choriocarcinoma cells". The Journal of Biological Chemistry. 276 (26): 23464–70. doi:10.1074/jbc.M010934200. PMID 11313339.
  34. ↑ Noland CL, Gierke S, Schnier PD, Murray J, Sandoval WN, Sagolla M, Dey A, Hannoush RN, Fairbrother WJ, Cunningham CN (January 2016). "Palmitoylation of TEAD Transcription Factors Is Required for Their Stability and Function in Hippo Pathway Signaling". Structure. 24 (1): 179–86. doi:10.1016/j.str.2015.11.005. PMID 26724994.
  35. ↑ Belandia B, Parker MG (October 2000). "Functional interaction between the p160 coactivator proteins and the transcriptional enhancer factor family of transcription factors". The Journal of Biological Chemistry. 275 (40): 30801–5. doi:10.1074/jbc.C000484200. PMID 10934189.
  36. ↑ Butler AJ, Ordahl CP (January 1999). "Poly(ADP-ribose) polymerase binds with transcription enhancer factor 1 to MCAT1 elements to regulate muscle-specific transcription". Molecular and Cellular Biology. 19 (1): 296–306. doi:10.1128/mcb.19.1.296. PMC 83887. PMID 9858553.
  37. ↑ MacLellan WR, Lee TC, Schwartz RJ, Schneider MD (June 1994). "Transforming growth factor-beta response elements of the skeletal alpha-actin gene. Combinatorial action of serum response factor, YY1, and the SV40 enhancer-binding protein, TEF-1". The Journal of Biological Chemistry. 269 (24): 16754–60. PMID 8206998.
  38. ↑ Maeda T, Chapman DL, Stewart AF (December 2002). "Mammalian vestigial-like 2, a cofactor of TEF-1 and MEF2 transcription factors that promotes skeletal muscle differentiation". The Journal of Biological Chemistry. 277 (50): 48889–98. doi:10.1074/jbc.M206858200. PMID 12376544.
  39. ↑ Gupta MP, Amin CS, Gupta M, Hay N, Zak R (July 1997). "Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression". Molecular and Cellular Biology. 17 (7): 3924–36. doi:10.1128/mcb.17.7.3924. PMC 232245. PMID 9199327.
  40. ↑ Chen L, Chan SW, Zhang X, Walsh M, Lim CJ, Hong W, Song H (February 2010). "Structural basis of YAP recognition by TEAD4 in the hippo pathway". Genes & Development. 24 (3): 290–300. doi:10.1101/gad.1865310. PMC 2811830. PMID 20123908.
  41. ↑ Pobbati AV, Chan SW, Lee I, Song H, Hong W (July 2012). "Structural and functional similarity between the Vgll1-TEAD and the YAP-TEAD complexes". Structure. 20 (7): 1135–40. doi:10.1016/j.str.2012.04.004. PMID 22632831.
  42. ↑ Günther S, Mielcarek M, Krüger M, Braun T (2004). "VITO-1 is an essential cofactor of TEF1-dependent muscle-specific gene regulation". Nucleic Acids Research. 32 (2): 791–802. doi:10.1093/nar/gkh248. PMC 373362. PMID 14762206.
  43. ↑ 43.0 43.1 Koontz LM, Liu-Chittenden Y, Yin F, Zheng Y, Yu J, Huang B, Chen Q, Wu S, Pan D (May 2013). "The Hippo effector Yorkie controls normal tissue growth by antagonizing scalloped-mediated default repression". Developmental Cell. 25 (4): 388–401. doi:10.1016/j.devcel.2013.04.021. PMC 3705890. PMID 23725764.
  44. ↑ Vassilev A, Kaneko KJ, Shu H, Zhao Y, DePamphilis ML (May 2001). "TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm". Genes & Development. 15 (10): 1229–41. doi:10.1101/gad.888601. PMC 313800. PMID 11358867.
  45. ↑ Zhao B, Li L, Lei Q, Guan KL (May 2010). "The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version". Genes & Development. 24 (9): 862–74. doi:10.1101/gad.1909210. PMC 2861185. PMID 20439427.
  46. ↑ Han W, Jung EM, Cho J, Lee JW, Hwang KT, Yang SJ, Kang JJ, Bae JY, Jeon YK, Park IA, Nicolau M, Jeffrey SS, Noh DY (June 2008). "DNA copy number alterations and expression of relevant genes in triple-negative breast cancer". Genes, Chromosomes & Cancer. 47 (6): 490–9. doi:10.1002/gcc.20550. PMID 18314908.
  47. ↑ Richardson AL, Wang ZC, De Nicolo A, Lu X, Brown M, Miron A, Liao X, Iglehart JD, Livingston DM, Ganesan S (February 2006). "X chromosomal abnormalities in basal-like human breast cancer". Cancer Cell. 9 (2): 121–32. doi:10.1016/j.ccr.2006.01.013. PMID 16473279.
  48. ↑ Nowee ME, Snijders AM, Rockx DA, de Wit RM, Kosma VM, Hämäläinen K, Schouten JP, Verheijen RH, van Diest PJ, Albertson DG, Dorsman JC (September 2007). "DNA profiling of primary serous ovarian and fallopian tube carcinomas with array comparative genomic hybridization and multiplex ligation-dependent probe amplification". The Journal of Pathology. 213 (1): 46–55. doi:10.1002/path.2217. PMID 17668415.
  49. ↑ Skotheim RI, Autio R, Lind GE, Kraggerud SM, Andrews PW, Monni O, Kallioniemi O, Lothe RA (2006). "Novel genomic aberrations in testicular germ cell tumors by array-CGH, and associated gene expression changes". Cellular Oncology. 28 (5–6): 315–26. PMC 4615958. PMID 17167184.
  50. ↑ Landin Malt A, Cagliero J, Legent K, Silber J, Zider A, Flagiello D (2012). "Alteration of TEAD1 expression levels confers apoptotic resistance through the transcriptional up-regulation of Livin". PLoS One. 7 (9): e45498. doi:10.1371/journal.pone.0045498. PMC 3454436. PMID 23029054.
  51. ↑ Xia Y, Zhang YL, Yu C, Chang T, Fan HY (2014). "YAP/TEAD co-activator regulated pluripotency and chemoresistance in ovarian cancer initiated cells". PLoS One. 9 (11): e109575. doi:10.1371/journal.pone.0109575. PMC 4219672. PMID 25369529.
  52. ↑ Yuan H, Liu H, Liu Z, Zhu D, Amos CI, Fang S, Lee JE, Wei Q (August 2015). "Genetic variants in Hippo pathway genes YAP1, TEAD1 and TEAD4 are associated with melanoma-specific survival". International Journal of Cancer. 137 (3): 638–45. doi:10.1002/ijc.29429. PMC 4437894. PMID 25628125.

Further reading

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