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{{Infobox_gene}}
{{PBB_Controls
'''Adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 1 (APPL1)''', or DCC-interacting protein 13-alpha (DIP13alpha), is a [[protein]] that in humans is encoded by the ''APPL1'' [[gene]].<ref name="pmid10490823">{{cite journal | vauthors = Mitsuuchi Y, Johnson SW, Sonoda G, Tanno S, Golemis EA, Testa JR | title = Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2 | journal = Oncogene | volume = 18 | issue = 35 | pages = 4891–8 | date = September 1999 | pmid = 10490823 | pmc =  | doi = 10.1038/sj.onc.1203080 }}</ref><ref name="pmid17030088">{{cite journal | vauthors = Nechamen CA, Thomas RM, Dias JA | title = APPL1, APPL2, Akt2 and FOXO1a interact with FSHR in a potential signaling complex | journal = Molecular and Cellular Endocrinology | volume = 260-262 | issue =  | pages = 93–9 | date = January 2007 | pmid = 17030088 | pmc = 1782224 | doi = 10.1016/j.mce.2006.08.014 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: APPL1 adaptor protein, phosphotyrosine interaction, PH domain and leucine zipper containing 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26060| accessdate = }}</ref> APPL1 contains several key interactory domains: [[Pleckstrin homology domain|pleckstrin homology (PH) domain]], [[Phosphotyrosine-binding domain|phosphotyrosine-binding (PTB) domain]] and [[BAR domain|Bin–Amphiphysin–Rvs]] (BAR) domain.<ref name="Diggins_2017">{{cite journal | vauthors = Diggins NL, Webb DJ | title = APPL1 is a multifunctional endosomal signaling adaptor protein | language = en | journal = Biochemical Society Transactions | volume = 45 | issue = 3 | pages = 771–779 | date = June 2017 | pmid = 28620038 | doi = 10.1042/bst20160191 }}</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
APPL1 is an [[Vesicular transport adaptor protein|adaptor protein]] localized to a subset of [[Rab5]]-positive ("early") [[endosome]]s, where it recruits other binding partners and regulates [[vesicle trafficking]] and endosomal [[Cell signaling|signalling]]. APPL1 is enriched at very early endosomes which are negative for [[EEA1]], indicating that APPL1 affects the earliest stages of endosomal traffic before EEA1 takes over. This is in line with observations that APPL1 and EEA1 compete for Rab5 binding. APPL1 affects the speed of internalization of key endosomal cargo (eg. [[Epidermal growth factor receptor|EGF receptor]]) which is dependent on Rab5 activation.<ref name="Diggins_2017" />
| image = PBB_Protein_APPL1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ela.
| PDB = {{PDB2|2ela}}, {{PDB2|2elb}}
| Name = Adaptor protein, phosphotyrosine interaction, PH domain and leucine zipper containing 1
| HGNCid = 24035
| Symbol = APPL1
| AltSymbols =; APPL; DIP13alpha
| OMIM = 604299
| ECnumber = 
| Homologene = 32143
| MGIid = 1920243
| GeneAtlas_image1 = PBB_GE_APPL1_218158_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0010008 |text = endosome membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016581 |text = NuRD complex}}
| Process = {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 26060
    | Hs_Ensembl = ENSG00000157500
    | Hs_RefseqProtein = NP_036228
    | Hs_RefseqmRNA = NM_012096
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 57236894
    | Hs_GenLoc_end = 57282536
    | Hs_Uniprot = Q9UKG1
    | Mm_EntrezGene = 72993
    | Mm_Ensembl = ENSMUSG00000040760
    | Mm_RefseqmRNA = XM_975639
    | Mm_RefseqProtein = XP_980733
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 25745872
    | Mm_GenLoc_end = 25797435
    | Mm_Uniprot = Q8K3H0
  }}
}}
'''Adaptor protein, phosphotyrosine interaction, PH domain and leucine zipper containing 1''', also known as '''APPL1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: APPL1 adaptor protein, phosphotyrosine interaction, PH domain and leucine zipper containing 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26060| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
PTB domain of APPL1 regulates many cell signalling events in specific endosomal compartments - sometimes termed the "signalling endosomes". This includes [[lysophosphatidic acid]] (LPA)-induced signaling (together with interacting protein [[GIPC1]]). Additional roles for APPL1 were pinpointed to the [[Cell nucleus|nucleus]] where APPL1 can localize once dissociated from endosomes.<ref name="Diggins_2017" />
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene has been shown to be involved in the regulation of cell proliferation, and in the crosstalk between the adiponectin signalling and insulin signalling pathways. The encoded protein binds many other proteins, including RAB5A, DCC, AKT2, PIK3CA, adiponectin receptors, and proteins of the NuRD/MeCP1 complex. This protein is found associated with endosomal membranes, but can be released by EGF and translocated to the nucleus.<ref name="entrez">{{cite web | title = Entrez Gene: APPL1 adaptor protein, phosphotyrosine interaction, PH domain and leucine zipper containing 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26060| accessdate = }}</ref>
}}


==References==
== Mutant studies ==
{{reflist|2}}
{| class="wikitable"
==Further reading==
|-
! colspan=3 | Mouse Mutant Alleles for Appl1
|-
| Marker Symbol for Mouse Gene. This symbol is assigned to the genomic locus by the [http://informatics.jax.org MGI]||[http://www.informatics.jax.org/javawi2/servlet/WIFetch?page=markerDetail&key=56973 Appl1]
|-
| Mutant Mouse Embryonic Stem Cell Clones. These are the known targeted mutations for this gene in a mouse.||[http://www.knockoutmouse.org/genedetails/MGI:1920243 Appl1<sup>tm1a(KOMP)Wtsi</sup>]
|-
| colspan=2 | '''Example structure of targeted conditional mutant allele for this gene'''
|-
| colspan=2 | [[File:Appl1 tm1a(KOMP)Wtsi.jpg|720px|Molecular structure of Appl1 region with inserted mutation sequence]]
|-
| colspan=2 | These Mutant ES Cells can be studied directly or used to generate mice with this gene knocked out. Study of these mice can shed light on the function of Appl1:
see [[Knockout mouse]]
|}
 
== Interactions ==
 
APPL1 has been shown to [[Protein-protein interaction|interact]] with [[Deleted in Colorectal Cancer]],<ref name=pmid12011067>{{cite journal | vauthors = Liu J, Yao F, Wu R, Morgan M, Thorburn A, Finley RL, Chen YQ | title = Mediation of the DCC apoptotic signal by DIP13 alpha | journal = The Journal of Biological Chemistry | volume = 277 | issue = 29 | pages = 26281–5 | date = July 2002 | pmid = 12011067 | doi = 10.1074/jbc.M204679200 }}</ref> [[AKT2]],<ref name=pmid10490823 /> but also [[Rab5]], [[RAB21|Rab21]], [[OCRL]] and almost 30 other proteins.<ref name="Diggins_2017" />
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T | title = Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones | journal = DNA Research | volume = 9 | issue = 3 | pages = 99–106 | date = June 2002 | pmid = 12168954 | doi = 10.1093/dnares/9.3.99 }}
| citations =
* {{cite journal | vauthors = Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Research | volume = 7 | issue = 1 | pages = 65–73 | date = February 2000 | pmid = 10718198 | doi = 10.1093/dnares/7.1.65 }}
*{{cite journal | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi= }}
* {{cite journal | vauthors = Liu J, Yao F, Wu R, Morgan M, Thorburn A, Finley RL, Chen YQ | title = Mediation of the DCC apoptotic signal by DIP13 alpha | journal = The Journal of Biological Chemistry | volume = 277 | issue = 29 | pages = 26281–5 | date = July 2002 | pmid = 12011067 | doi = 10.1074/jbc.M204679200 }}
*{{cite journal  | author=Mitsuuchi Y, Johnson SW, Sonoda G, ''et al.'' |title=Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2. |journal=Oncogene |volume=18 |issue= 35 |pages= 4891-8 |year= 1999 |pmid= 10490823 |doi= 10.1038/sj.onc.1203080 }}
* {{cite journal | vauthors = Yang L, Lin HK, Altuwaijri S, Xie S, Wang L, Chang C | title = APPL suppresses androgen receptor transactivation via potentiating Akt activity | journal = The Journal of Biological Chemistry | volume = 278 | issue = 19 | pages = 16820–7 | date = May 2003 | pmid = 12621049 | doi = 10.1074/jbc.M213163200 }}
*{{cite journal | author=Nagase T, Kikuno R, Ishikawa KI, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=7 |issue= 1 |pages= 65-73 |year= 2000 |pmid= 10718198 |doi= }}
* {{cite journal | vauthors = Miaczynska M, Christoforidis S, Giner A, Shevchenko A, Uttenweiler-Joseph S, Habermann B, Wilm M, Parton RG, Zerial M | title = APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment | journal = Cell | volume = 116 | issue = 3 | pages = 445–56 | date = February 2004 | pmid = 15016378 | doi = 10.1016/S0092-8674(04)00117-5 }}
*{{cite journal | author=Liu J, Yao F, Wu R, ''et al.'' |title=Mediation of the DCC apoptotic signal by DIP13 alpha. |journal=J. Biol. Chem. |volume=277 |issue= 29 |pages= 26281-5 |year= 2002 |pmid= 12011067 |doi= 10.1074/jbc.M204679200 }}
* {{cite journal | vauthors = Nechamen CA, Thomas RM, Cohen BD, Acevedo G, Poulikakos PI, Testa JR, Dias JA | title = Human follicle-stimulating hormone (FSH) receptor interacts with the adaptor protein APPL1 in HEK 293 cells: potential involvement of the PI3K pathway in FSH signaling | journal = Biology of Reproduction | volume = 71 | issue = 2 | pages = 629–36 | date = August 2004 | pmid = 15070827 | doi = 10.1095/biolreprod.103.025833 }}
*{{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 = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = August 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 }}
*{{cite journal  | author=Yang L, Lin HK, Altuwaijri S, ''et al.'' |title=APPL suppresses androgen receptor transactivation via potentiating Akt activity. |journal=J. Biol. Chem. |volume=278 |issue= 19 |pages= 16820-7 |year= 2003 |pmid= 12621049 |doi= 10.1074/jbc.M213163200 }}
* {{cite journal | vauthors = Ballif BA, Villén J, Beausoleil SA, Schwartz D, Gygi SP | title = Phosphoproteomic analysis of the developing mouse brain | journal = Molecular & Cellular Proteomics | volume = 3 | issue = 11 | pages = 1093–101 | date = November 2004 | pmid = 15345747 | doi = 10.1074/mcp.M400085-MCP200 }}
*{{cite journal | author=Miaczynska M, Christoforidis S, Giner A, ''et al.'' |title=APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment. |journal=Cell |volume=116 |issue= 3 |pages= 445-56 |year= 2004 |pmid= 15016378 |doi= }}
* {{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 | volume = 437 | issue = 7062 | pages = 1173–8 | date = October 2005 | pmid = 16189514 | doi = 10.1038/nature04209 }}
*{{cite journal | author=Nechamen CA, Thomas RM, Cohen BD, ''et al.'' |title=Human follicle-stimulating hormone (FSH) receptor interacts with the adaptor protein APPL1 in HEK 293 cells: potential involvement of the PI3K pathway in FSH signaling. |journal=Biol. Reprod. |volume=71 |issue= 2 |pages= 629-36 |year= 2005 |pmid= 15070827 |doi= 10.1095/biolreprod.103.025833 }}
* {{cite journal | vauthors = Mao X, Kikani CK, Riojas RA, Langlais P, Wang L, Ramos FJ, Fang Q, Christ-Roberts CY, Hong JY, Kim RY, Liu F, Dong LQ | title = APPL1 binds to adiponectin receptors and mediates adiponectin signalling and function | journal = Nature Cell Biology | volume = 8 | issue = 5 | pages = 516–23 | date = May 2006 | pmid = 16622416 | doi = 10.1038/ncb1404 }}
*{{cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
* {{cite journal | vauthors = Cheng KK, Lam KS, Wang Y, Huang Y, Carling D, Wu D, Wong C, Xu A | title = Adiponectin-induced endothelial nitric oxide synthase activation and nitric oxide production are mediated by APPL1 in endothelial cells | journal = Diabetes | volume = 56 | issue = 5 | pages = 1387–94 | date = May 2007 | pmid = 17287464 | doi = 10.2337/db06-1580 }}
*{{cite journal | author=Ballif BA, Villén J, Beausoleil SA, ''et al.'' |title=Phosphoproteomic analysis of the developing mouse brain. |journal=Mol. Cell Proteomics |volume=3 |issue= 11 |pages= 1093-101 |year= 2005 |pmid= 15345747 |doi= 10.1074/mcp.M400085-MCP200 }}
* {{cite journal | vauthors = Li J, Mao X, Dong LQ, Liu F, Tong L | title = Crystal structures of the BAR-PH and PTB domains of human APPL1 | journal = Structure | volume = 15 | issue = 5 | pages = 525–33 | date = May 2007 | pmid = 17502098 | doi = 10.1016/j.str.2007.03.011 }}
*{{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 }}
* {{cite journal | vauthors = Zhu G, Chen J, Liu J, Brunzelle JS, Huang B, Wakeham N, Terzyan S, Li X, Rao Z, Li G, Zhang XC | title = Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5 | journal = The EMBO Journal | volume = 26 | issue = 14 | pages = 3484–93 | date = July 2007 | pmid = 17581628 | pmc = 1933402 | doi = 10.1038/sj.emboj.7601771 }}
*{{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 | vauthors = Saito T, Jones CC, Huang S, Czech MP, Pilch PF | title = The interaction of Akt with APPL1 is required for insulin-stimulated Glut4 translocation | journal = The Journal of Biological Chemistry | volume = 282 | issue = 44 | pages = 32280–7 | date = November 2007 | pmid = 17848569 | doi = 10.1074/jbc.M704150200 }}
*{{cite journal | author=Mao X, Kikani CK, Riojas RA, ''et al.'' |title=APPL1 binds to adiponectin receptors and mediates adiponectin signalling and function. |journal=Nat. Cell Biol. |volume=8 |issue= 5 |pages= 516-23 |year= 2006 |pmid= 16622416 |doi= 10.1038/ncb1404 }}
*{{cite journal | author=Nechamen CA, Thomas RM, Dias JA |title=APPL1, APPL2, Akt2 and FOXO1a interact with FSHR in a potential signaling complex. |journal=Mol. Cell. Endocrinol. |volume=260-262 |issue=  |pages= 93-9 |year= 2007 |pmid= 17030088 |doi= 10.1016/j.mce.2006.08.014 }}
*{{cite journal  | author=Cheng KK, Lam KS, Wang Y, ''et al.'' |title=Adiponectin-induced endothelial nitric oxide synthase activation and nitric oxide production are mediated by APPL1 in endothelial cells. |journal=Diabetes |volume=56 |issue= 5 |pages= 1387-94 |year= 2007 |pmid= 17287464 |doi= 10.2337/db06-1580 }}
*{{cite journal | author=Li J, Mao X, Dong LQ, ''et al.'' |title=Crystal structures of the BAR-PH and PTB domains of human APPL1. |journal=Structure |volume=15 |issue= 5 |pages= 525-33 |year= 2007 |pmid= 17502098 |doi= 10.1016/j.str.2007.03.011 }}
*{{cite journal | author=Zhu G, Chen J, Liu J, ''et al.'' |title=Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5. |journal=EMBO J. |volume=26 |issue= 14 |pages= 3484-93 |year= 2007 |pmid= 17581628 |doi= 10.1038/sj.emboj.7601771 }}
*{{cite journal | author=Saito T, Jones CC, Huang S, ''et al.'' |title=The interaction of Akt with APPL1 is required for insulin-stimulated Glut4 translocation. |journal=J. Biol. Chem. |volume=282 |issue= 44 |pages= 32280-7 |year= 2007 |pmid= 17848569 |doi= 10.1074/jbc.M704150200 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{WikiDoc Sources}}
* {{UCSC gene info|APPL1}}
 
{{PDB Gallery|geneid=26060}}
 
 
{{gene-3-stub}}

Latest revision as of 02:26, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

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

Adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 1 (APPL1), or DCC-interacting protein 13-alpha (DIP13alpha), is a protein that in humans is encoded by the APPL1 gene.[1][2][3] APPL1 contains several key interactory domains: pleckstrin homology (PH) domain, phosphotyrosine-binding (PTB) domain and Bin–Amphiphysin–Rvs (BAR) domain.[4]

Function

APPL1 is an adaptor protein localized to a subset of Rab5-positive ("early") endosomes, where it recruits other binding partners and regulates vesicle trafficking and endosomal signalling. APPL1 is enriched at very early endosomes which are negative for EEA1, indicating that APPL1 affects the earliest stages of endosomal traffic before EEA1 takes over. This is in line with observations that APPL1 and EEA1 compete for Rab5 binding. APPL1 affects the speed of internalization of key endosomal cargo (eg. EGF receptor) which is dependent on Rab5 activation.[4]

PTB domain of APPL1 regulates many cell signalling events in specific endosomal compartments - sometimes termed the "signalling endosomes". This includes lysophosphatidic acid (LPA)-induced signaling (together with interacting protein GIPC1). Additional roles for APPL1 were pinpointed to the nucleus where APPL1 can localize once dissociated from endosomes.[4]

Mutant studies

Mouse Mutant Alleles for Appl1
Marker Symbol for Mouse Gene. This symbol is assigned to the genomic locus by the MGI Appl1
Mutant Mouse Embryonic Stem Cell Clones. These are the known targeted mutations for this gene in a mouse. Appl1tm1a(KOMP)Wtsi
Example structure of targeted conditional mutant allele for this gene
Molecular structure of Appl1 region with inserted mutation sequence
These Mutant ES Cells can be studied directly or used to generate mice with this gene knocked out. Study of these mice can shed light on the function of Appl1:

see Knockout mouse

Interactions

APPL1 has been shown to interact with Deleted in Colorectal Cancer,[5] AKT2,[1] but also Rab5, Rab21, OCRL and almost 30 other proteins.[4]

References

  1. ↑ 1.0 1.1 Mitsuuchi Y, Johnson SW, Sonoda G, Tanno S, Golemis EA, Testa JR (September 1999). "Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2". Oncogene. 18 (35): 4891–8. doi:10.1038/sj.onc.1203080. PMID 10490823.
  2. ↑ Nechamen CA, Thomas RM, Dias JA (January 2007). "APPL1, APPL2, Akt2 and FOXO1a interact with FSHR in a potential signaling complex". Molecular and Cellular Endocrinology. 260-262: 93–9. doi:10.1016/j.mce.2006.08.014. PMC 1782224. PMID 17030088.
  3. ↑ "Entrez Gene: APPL1 adaptor protein, phosphotyrosine interaction, PH domain and leucine zipper containing 1".
  4. ↑ 4.0 4.1 4.2 4.3 Diggins NL, Webb DJ (June 2017). "APPL1 is a multifunctional endosomal signaling adaptor protein". Biochemical Society Transactions. 45 (3): 771–779. doi:10.1042/bst20160191. PMID 28620038.
  5. ↑ Liu J, Yao F, Wu R, Morgan M, Thorburn A, Finley RL, Chen YQ (July 2002). "Mediation of the DCC apoptotic signal by DIP13 alpha". The Journal of Biological Chemistry. 277 (29): 26281–5. doi:10.1074/jbc.M204679200. PMID 12011067.

Further reading

  • Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (June 2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Research. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
  • Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O (February 2000). "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 7 (1): 65–73. doi:10.1093/dnares/7.1.65. PMID 10718198.
  • Liu J, Yao F, Wu R, Morgan M, Thorburn A, Finley RL, Chen YQ (July 2002). "Mediation of the DCC apoptotic signal by DIP13 alpha". The Journal of Biological Chemistry. 277 (29): 26281–5. doi:10.1074/jbc.M204679200. PMID 12011067.
  • Yang L, Lin HK, Altuwaijri S, Xie S, Wang L, Chang C (May 2003). "APPL suppresses androgen receptor transactivation via potentiating Akt activity". The Journal of Biological Chemistry. 278 (19): 16820–7. doi:10.1074/jbc.M213163200. PMID 12621049.
  • Miaczynska M, Christoforidis S, Giner A, Shevchenko A, Uttenweiler-Joseph S, Habermann B, Wilm M, Parton RG, Zerial M (February 2004). "APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment". Cell. 116 (3): 445–56. doi:10.1016/S0092-8674(04)00117-5. PMID 15016378.
  • Nechamen CA, Thomas RM, Cohen BD, Acevedo G, Poulikakos PI, Testa JR, Dias JA (August 2004). "Human follicle-stimulating hormone (FSH) receptor interacts with the adaptor protein APPL1 in HEK 293 cells: potential involvement of the PI3K pathway in FSH signaling". Biology of Reproduction. 71 (2): 629–36. doi:10.1095/biolreprod.103.025833. PMID 15070827.
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Ballif BA, Villén J, Beausoleil SA, Schwartz D, Gygi SP (November 2004). "Phosphoproteomic analysis of the developing mouse brain". Molecular & Cellular Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
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External links


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