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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Adrenocortical dysplasia protein homolog''' is a [[protein]] that in humans is encoded by the ''ACD'' [[gene]].<ref name="pmid15231715">{{cite journal | vauthors = Ye JZ, Hockemeyer D, Krutchinsky AN, Loayza D, Hooper SM, Chait BT, de Lange T | title = POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex | journal = Genes Dev | volume = 18 | issue = 14 | pages = 1649–54 | date = July 2004 | pmid = 15231715 | pmc = 478187 | doi = 10.1101/gad.1215404 }}</ref><ref name="pmid15181449">{{cite journal | vauthors = Liu D, Safari A, O'Connor MS, Chan DW, Laegeler A, Qin J, Songyang Z | title = PTOP interacts with POT1 and regulates its localization to telomeres | journal = Nat Cell Biol | volume = 6 | issue = 7 | pages = 673–80 | date = July 2004 | pmid = 15181449 | pmc = | doi = 10.1038/ncb1142 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ACD adrenocortical dysplasia homolog (mouse)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=65057| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_ACD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2i46.
| PDB = {{PDB2|2i46}}
| Name = Adrenocortical dysplasia homolog (mouse)
| HGNCid = 25070
| Symbol = ACD
| AltSymbols =; TPP1; PIP1; PTOP; TINT1
| OMIM = 609377
| ECnumber = 
| Homologene = 23391
| MGIid = 87873
| GeneAtlas_image1 = PBB_GE_ACD_204617_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}}
| Component = {{GNF_GO|id=GO:0000781 |text = chromosome, telomeric region}} {{GNF_GO|id=GO:0000783 |text = nuclear telomere cap complex}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}}
| Process = {{GNF_GO|id=GO:0000723 |text = telomere maintenance}} {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0001655 |text = urogenital system development}} {{GNF_GO|id=GO:0030326 |text = embryonic limb morphogenesis}} {{GNF_GO|id=GO:0035282 |text = segmentation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 65057
    | Hs_Ensembl = ENSG00000102977
    | Hs_RefseqProtein = NP_075065
    | Hs_RefseqmRNA = NM_022914
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 66248934
    | Hs_GenLoc_end = 66252214
    | Hs_Uniprot = Q96AP0
    | Mm_EntrezGene = 497652
    | Mm_Ensembl = ENSMUSG00000038000
    | Mm_RefseqmRNA = NM_001012638
    | Mm_RefseqProtein = NP_001012656
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 108584989
    | Mm_GenLoc_end = 108590214
    | Mm_Uniprot = Q5EE38
  }}
}}
'''Adrenocortical dysplasia homolog (mouse)''', also known as '''ACD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACD adrenocortical dysplasia homolog (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=65057| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a protein that is involved in telomere function. This protein is one of six core proteins in the telosome/shelterin telomeric complex, which functions to maintain telomere length and to protect telomere ends. Through its interaction with other components, this protein plays a key role in the assembly and stabilization of this complex, and it mediates the access of telomerase to the telomere. Multiple transcript variants encoding different isoforms have been found for this gene. This gene, which is also referred to as TPP1, is distinct from the unrelated TPP1 gene on chromosome 11, which encodes tripeptidyl-peptidase I.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein that is involved in telomere function. This protein is one of six core proteins in the telosome/shelterin telomeric complex, which functions to maintain telomere length and to protect telomere ends. Through its interaction with other components, this protein plays a key role in the assembly and stabilization of this complex, and it mediates the access of telomerase to the telomere. Multiple transcript variants encoding different isoforms have been found for this gene. This gene, which is also referred to as TPP1, is distinct from the unrelated TPP1 gene on chromosome 11, which encodes tripeptidyl-peptidase I.<ref name="entrez">{{cite web | title = Entrez Gene: ACD adrenocortical dysplasia homolog (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=65057| accessdate = }}</ref>
}}


==References==
TPP1 is a component of the telomere-specific [[shelterin]] complex, which facilitats the replication of the double-stranded telomeric DNA tracts and protects the telomeric end from unregulated DNA repair activities. TPP1 mainly functions as a regulator of telomerase recruitment, activation, and regulation.<ref name="pmid25184673">{{cite journal|date=September 2014|title=Modern genome editing meets telomeres: the many functions of TPP1|journal=Genes & Development|volume=28|issue=17|pages=1857–8|doi=10.1101/gad.250316.114|pmc=4197952|pmid=25184673|vauthors=Karlseder J}}</ref> Although TPP1 was originally described as a bridging factor between [[TRF1]] and [[TRF2]], which participate in a pathway with [[POT1]] as a negative regulator of telomerase-dependent telomere length control, <ref name="pmid17632522">{{cite journal|date=August 2007|title=Telomere protection by mammalian Pot1 requires interaction with Tpp1|journal=Nature Structural & Molecular Biology|volume=14|issue=8|pages=754–61|doi=10.1038/nsmb1270|pmid=17632522|vauthors=Hockemeyer D, Palm W, Else T, Daniels JP, Takai KK, Ye JZ, Keegan CE, de Lange T, Hammer GD}}</ref> more recent studies suggest that TPP1 could directly promotes telomerase activity at the telomere.<ref name="pmid23103865">{{cite journal|date=December 2012|title=The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity|journal=Nature|volume=492|issue=7428|pages=285–9|doi=10.1038/nature11648|pmc=3521872|pmid=23103865|vauthors=Nandakumar J, Bell CF, Weidenfeld I, Zaug AJ, Leinwand LA, Cech TR}}</ref> A part of the TPP1 oligonucleotide/oligosaccharide-binding (OB) fold named [[TEL patch]] that interacts with the catalytic subunit of telomerase, [[hTERT]], has been proven essential for telomerase activation.<ref name="pmid25128433">{{cite journal|date=September 2014|title=Genetic and molecular identification of three human TPP1 functions in telomerase action: recruitment, activation, and homeostasis set point regulation|journal=Genes & Development|volume=28|issue=17|pages=1885–99|doi=10.1101/gad.246819.114|pmc=4197946|pmid=25128433|vauthors=Sexton AN, Regalado SG, Lai CS, Cost GJ, O'Neil CM, Urnov FD, Gregory PD, Jaenisch R, Collins K, Hockemeyer D}}</ref> What’s more, TPP1 has been demonstrated the only pathway required for recruitment of telomerase to chromosome ends, and it also defines telomere length homeostasis in hESCs.<ref name="pmid25128433" />
{{reflist|2}}
 
==Further reading==
== Interactions ==
 
ACD (gene) has been shown to [[Protein-protein interaction|interact]] with [[POT1]]<ref name=pmid15231715 /><ref name=pmid15181449 /><ref name=pmid16189514>{{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = [[Nature (journal)|Nature]] | volume = 437 | issue = 7062 | pages = 1173–8 | date = October 2005 | pmid = 16189514 | doi = 10.1038/nature04209 }}</ref> and [[TINF2]].<ref name=pmid15231715/><ref name=pmid15181449/>
 
* POT1 <ref name="pmid19864690">{{cite journal|date=January 2010|title=In vivo stoichiometry of shelterin components|journal=The Journal of Biological Chemistry|volume=285|issue=2|pages=1457–67|doi=10.1074/jbc.M109.038026|pmc=2801271|pmid=19864690|vauthors=Takai KK, Hooper S, Blackwood S, Gandhi R, de Lange T}}</ref>
* hTERT  <ref name="pmid231038652">{{cite journal|date=December 2012|title=The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity|journal=Nature|volume=492|issue=7428|pages=285–9|doi=10.1038/nature11648|pmc=3521872|pmid=23103865|vauthors=Nandakumar J, Bell CF, Weidenfeld I, Zaug AJ, Leinwand LA, Cech TR}}</ref> <ref name="pmid176325222">{{cite journal|date=August 2007|title=Telomere protection by mammalian Pot1 requires interaction with Tpp1|journal=Nature Structural & Molecular Biology|volume=14|issue=8|pages=754–61|doi=10.1038/nsmb1270|pmid=17632522|vauthors=Hockemeyer D, Palm W, Else T, Daniels JP, Takai KK, Ye JZ, Keegan CE, de Lange T, Hammer GD}}</ref>
* [[TIN2]] <ref name="pmid16880378">{{cite journal|date=August 2006|title=A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly|journal=Proceedings of the National Academy of Sciences of the United States of America|volume=103|issue=32|pages=11874–9|doi=10.1073/pnas.0605303103|pmc=1567669|pmid=16880378|vauthors=O'Connor MS, Safari A, Xin H, Liu D, Songyang Z}}</ref>
* TRF1 <ref name="pmid16880378" />
* TRF2 <ref name="pmid16880378" />
* [[Telomerase]] <ref name="pmid20231318">{{cite journal|date=March 2010|title=Functional interaction between telomere protein TPP1 and telomerase|journal=Genes & Development|volume=24|issue=6|pages=613–22|doi=10.1101/gad.1881810|pmc=2841338|pmid=20231318|vauthors=Zaug AJ, Podell ER, Nandakumar J, Cech TR}}</ref>
 
== References ==
{{reflist}}
 
==External links==
* {{UCSC gene info|ACD}}
* {{UCSC gene info|TPP1}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = de Lange T | title = Shelterin: the protein complex that shapes and safeguards human telomeres. | journal = Genes Dev. | volume = 19 | issue = 18 | pages = 2100–10 | year = 2005 | pmid = 16166375 | doi = 10.1101/gad.1346005 }}
| citations =
* {{cite journal | vauthors = Songyang Z, Liu D | title = Inside the mammalian telomere interactome: regulation and regulatory activities of telomeres. | journal = Crit. Rev. Eukaryot. Gene Expr. | volume = 16 | issue = 2 | pages = 103–18 | year = 2006 | pmid = 16749892 | doi = 10.1615/critreveukargeneexpr.v16.i2.10 }}
*{{cite journal | author=de Lange T |title=Shelterin: the protein complex that shapes and safeguards human telomeres. |journal=Genes Dev. |volume=19 |issue= 18 |pages= 2100-10 |year= 2005 |pmid= 16166375 |doi= 10.1101/gad.1346005 }}
* {{cite journal | vauthors = Cristofari G, Sikora K, Lingner J | title = Telomerase unplugged. | journal = ACS Chem. Biol. | volume = 2 | issue = 3 | pages = 155–8 | year = 2007 | pmid = 17373762 | doi = 10.1021/cb700037c }}
*{{cite journal | author=Songyang Z, Liu D |title=Inside the mammalian telomere interactome: regulation and regulatory activities of telomeres. |journal=Crit. Rev. Eukaryot. Gene Expr. |volume=16 |issue= 2 |pages= 103-18 |year= 2006 |pmid= 16749892 |doi= }}
* {{cite journal | vauthors = Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA | title = A "double adaptor" method for improved shotgun library construction. | journal = Anal. Biochem. | volume = 236 | issue = 1 | pages = 107–13 | year = 1996 | pmid = 8619474 | doi = 10.1006/abio.1996.0138 }}
*{{cite journal | author=Cristofari G, Sikora K, Lingner J |title=Telomerase unplugged. |journal=ACS Chem. Biol. |volume=2 |issue= 3 |pages= 155-8 |year= 2007 |pmid= 17373762 |doi= 10.1021/cb700037c }}
* {{cite journal | vauthors = Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA | title = Large-scale concatenation cDNA sequencing. | journal = Genome Res. | volume = 7 | issue = 4 | pages = 353–8 | year = 1997 | pmid = 9110174 | pmc = 139146 | doi = 10.1101/gr.7.4.353 }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
* {{cite journal | vauthors = Houghtaling BR, Cuttonaro L, Chang W, Smith S | title = A dynamic molecular link between the telomere length regulator TRF1 and the chromosome end protector TRF2. | journal = Curr. Biol. | volume = 14 | issue = 18 | pages = 1621–31 | year = 2005 | pmid = 15380063 | doi = 10.1016/j.cub.2004.08.052 }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi=  }}
* {{cite journal | vauthors = Keegan CE, Hutz JE, Else T, Adamska M, Shah SP, Kent AE, Howes JM, Beamer WG, Hammer GD | title = Urogenital and caudal dysgenesis in adrenocortical dysplasia (acd) mice is caused by a splicing mutation in a novel telomeric regulator. | journal = Hum. Mol. Genet. | volume = 14 | issue = 1 | pages = 113–23 | year = 2005 | pmid = 15537664 | doi = 10.1093/hmg/ddi011 }}
*{{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 | vauthors = Hutz JE, Krause AS, Achermann JC, Vilain E, Tauber M, Lecointre C, McCabe ER, Hammer GD, Keegan CE | title = IMAGe association and congenital adrenal hypoplasia: no disease-causing mutations found in the ACD gene. | journal = Mol. Genet. Metab. | volume = 88 | issue = 1 | pages = 66–70 | year = 2006 | pmid = 16504561 | doi = 10.1016/j.ymgme.2006.01.006 }}
*{{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 | vauthors = Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY | title = A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. | journal = Cell | volume = 125 | issue = 4 | pages = 801–14 | year = 2006 | pmid = 16713569 | doi = 10.1016/j.cell.2006.03.032 }}
*{{cite journal  | author=Liu D, Safari A, O'Connor MS, ''et al.'' |title=PTOP interacts with POT1 and regulates its localization to telomeres. |journal=Nat. Cell Biol. |volume=6 |issue= 7 |pages= 673-80 |year= 2004 |pmid= 15181449 |doi= 10.1038/ncb1142 }}
* {{cite journal | vauthors = O'Connor MS, Safari A, Xin H, Liu D, Songyang Z | title = A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 103 | issue = 32 | pages = 11874–9 | year = 2006 | pmid = 16880378 | pmc = 1567669 | doi = 10.1073/pnas.0605303103 }}
*{{cite journal  | author=Ye JZ, Hockemeyer D, Krutchinsky AN, ''et al.'' |title=POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex. |journal=Genes Dev. |volume=18 |issue= 14 |pages= 1649-54 |year= 2004 |pmid= 15231715 |doi= 10.1101/gad.1215404 }}
* {{cite journal | vauthors = Xin H, Liu D, Wan M, Safari A, Kim H, Sun W, O'Connor MS, Songyang Z | title = TPP1 is a homologue of ciliate TEBP-beta and interacts with POT1 to recruit telomerase. | journal = Nature | volume = 445 | issue = 7127 | pages = 559–62 | year = 2007 | pmid = 17237767 | doi = 10.1038/nature05469 }}
*{{cite journal | author=Houghtaling BR, Cuttonaro L, Chang W, Smith S |title=A dynamic molecular link between the telomere length regulator TRF1 and the chromosome end protector TRF2. |journal=Curr. Biol. |volume=14 |issue= 18 |pages= 1621-31 |year= 2005 |pmid= 15380063 |doi= 10.1016/j.cub.2004.08.052 }}
* {{cite journal | vauthors = Wang F, Podell ER, Zaug AJ, Yang Y, Baciu P, Cech TR, Lei M | title = The POT1-TPP1 telomere complex is a telomerase processivity factor. | journal = Nature | volume = 445 | issue = 7127 | pages = 506–10 | year = 2007 | pmid = 17237768 | doi = 10.1038/nature05454 | url = https://deepblue.lib.umich.edu/bitstream/2027.42/62923/1/nature05454.pdf }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
{{refend}}
*{{cite journal  | author=Keegan CE, Hutz JE, Else T, ''et al.'' |title=Urogenital and caudal dysgenesis in adrenocortical dysplasia (acd) mice is caused by a splicing mutation in a novel telomeric regulator. |journal=Hum. Mol. Genet. |volume=14 |issue= 1 |pages= 113-23 |year= 2005 |pmid= 15537664 |doi= 10.1093/hmg/ddi011 }}
* {{cite journal | vauthors = Wang F, Podell ER, Zaug AJ, Yang Y, Baciu P, Cech TR, Lei M | title = The POT1-TPP1 telomere complex is a telomerase processivity factor. | journal = Nature | volume = 445 | issue = 7127 | pages = 506–10 | year = 2007 | pmid = 17237768 | doi = 10.1038/nature05454 | url = https://deepblue.lib.umich.edu/bitstream/2027.42/62923/1/nature05454.pdf }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal  | author=Hutz JE, Krause AS, Achermann JC, ''et al.'' |title=IMAGe association and congenital adrenal hypoplasia: no disease-causing mutations found in the ACD gene. |journal=Mol. Genet. Metab. |volume=88 |issue= 1 |pages= 66-70 |year= 2006 |pmid= 16504561 |doi= 10.1016/j.ymgme.2006.01.006 }}
*{{cite journal | author=Lim J, Hao T, Shaw C, ''et al.'' |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. |journal=Cell |volume=125 |issue= 4 |pages= 801-14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032 }}
*{{cite journal | author=O'Connor MS, Safari A, Xin H, ''et al.'' |title=A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=103 |issue= 32 |pages= 11874-9 |year= 2006 |pmid= 16880378 |doi= 10.1073/pnas.0605303103 }}
*{{cite journal | author=Xin H, Liu D, Wan M, ''et al.'' |title=TPP1 is a homologue of ciliate TEBP-beta and interacts with POT1 to recruit telomerase. |journal=Nature |volume=445 |issue= 7127 |pages= 559-62 |year= 2007 |pmid= 17237767 |doi= 10.1038/nature05469 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=65057}}
{{WikiDoc Sources}}
 
[[Category:Human proteins]]
[[Category:Telomeres]]
[[Category:Telomere-related genes]]
[[Category:Telomere-related proteins]]

Latest revision as of 09:17, 10 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Adrenocortical dysplasia protein homolog is a protein that in humans is encoded by the ACD gene.[1][2][3]

Function

This gene encodes a protein that is involved in telomere function. This protein is one of six core proteins in the telosome/shelterin telomeric complex, which functions to maintain telomere length and to protect telomere ends. Through its interaction with other components, this protein plays a key role in the assembly and stabilization of this complex, and it mediates the access of telomerase to the telomere. Multiple transcript variants encoding different isoforms have been found for this gene. This gene, which is also referred to as TPP1, is distinct from the unrelated TPP1 gene on chromosome 11, which encodes tripeptidyl-peptidase I.[3]

TPP1 is a component of the telomere-specific shelterin complex, which facilitats the replication of the double-stranded telomeric DNA tracts and protects the telomeric end from unregulated DNA repair activities. TPP1 mainly functions as a regulator of telomerase recruitment, activation, and regulation.[4] Although TPP1 was originally described as a bridging factor between TRF1 and TRF2, which participate in a pathway with POT1 as a negative regulator of telomerase-dependent telomere length control, [5] more recent studies suggest that TPP1 could directly promotes telomerase activity at the telomere.[6] A part of the TPP1 oligonucleotide/oligosaccharide-binding (OB) fold named TEL patch that interacts with the catalytic subunit of telomerase, hTERT, has been proven essential for telomerase activation.[7] What’s more, TPP1 has been demonstrated the only pathway required for recruitment of telomerase to chromosome ends, and it also defines telomere length homeostasis in hESCs.[7]

Interactions

ACD (gene) has been shown to interact with POT1[1][2][8] and TINF2.[1][2]

References

  1. ↑ 1.0 1.1 1.2 Ye JZ, Hockemeyer D, Krutchinsky AN, Loayza D, Hooper SM, Chait BT, de Lange T (July 2004). "POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex". Genes Dev. 18 (14): 1649–54. doi:10.1101/gad.1215404. PMC 478187. PMID 15231715.
  2. ↑ 2.0 2.1 2.2 Liu D, Safari A, O'Connor MS, Chan DW, Laegeler A, Qin J, Songyang Z (July 2004). "PTOP interacts with POT1 and regulates its localization to telomeres". Nat Cell Biol. 6 (7): 673–80. doi:10.1038/ncb1142. PMID 15181449.
  3. ↑ 3.0 3.1 "Entrez Gene: ACD adrenocortical dysplasia homolog (mouse)".
  4. ↑ Karlseder J (September 2014). "Modern genome editing meets telomeres: the many functions of TPP1". Genes & Development. 28 (17): 1857–8. doi:10.1101/gad.250316.114. PMC 4197952. PMID 25184673.
  5. ↑ Hockemeyer D, Palm W, Else T, Daniels JP, Takai KK, Ye JZ, Keegan CE, de Lange T, Hammer GD (August 2007). "Telomere protection by mammalian Pot1 requires interaction with Tpp1". Nature Structural & Molecular Biology. 14 (8): 754–61. doi:10.1038/nsmb1270. PMID 17632522.
  6. ↑ Nandakumar J, Bell CF, Weidenfeld I, Zaug AJ, Leinwand LA, Cech TR (December 2012). "The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity". Nature. 492 (7428): 285–9. doi:10.1038/nature11648. PMC 3521872. PMID 23103865.
  7. ↑ 7.0 7.1 Sexton AN, Regalado SG, Lai CS, Cost GJ, O'Neil CM, Urnov FD, Gregory PD, Jaenisch R, Collins K, Hockemeyer D (September 2014). "Genetic and molecular identification of three human TPP1 functions in telomerase action: recruitment, activation, and homeostasis set point regulation". Genes & Development. 28 (17): 1885–99. doi:10.1101/gad.246819.114. PMC 4197946. PMID 25128433.
  8. ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  9. ↑ Takai KK, Hooper S, Blackwood S, Gandhi R, de Lange T (January 2010). "In vivo stoichiometry of shelterin components". The Journal of Biological Chemistry. 285 (2): 1457–67. doi:10.1074/jbc.M109.038026. PMC 2801271. PMID 19864690.
  10. ↑ Nandakumar J, Bell CF, Weidenfeld I, Zaug AJ, Leinwand LA, Cech TR (December 2012). "The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity". Nature. 492 (7428): 285–9. doi:10.1038/nature11648. PMC 3521872. PMID 23103865.
  11. ↑ Hockemeyer D, Palm W, Else T, Daniels JP, Takai KK, Ye JZ, Keegan CE, de Lange T, Hammer GD (August 2007). "Telomere protection by mammalian Pot1 requires interaction with Tpp1". Nature Structural & Molecular Biology. 14 (8): 754–61. doi:10.1038/nsmb1270. PMID 17632522.
  12. ↑ 12.0 12.1 12.2 O'Connor MS, Safari A, Xin H, Liu D, Songyang Z (August 2006). "A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly". Proceedings of the National Academy of Sciences of the United States of America. 103 (32): 11874–9. doi:10.1073/pnas.0605303103. PMC 1567669. PMID 16880378.
  13. ↑ Zaug AJ, Podell ER, Nandakumar J, Cech TR (March 2010). "Functional interaction between telomere protein TPP1 and telomerase". Genes & Development. 24 (6): 613–22. doi:10.1101/gad.1881810. PMC 2841338. PMID 20231318.

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Further reading

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