Biology:AP2B1
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
AP-2 complex subunit beta is a protein that in humans is encoded by the AP2B1 gene.[1][2][3]
Function
The protein encoded by this gene is one of two large chain components of the AP2 adaptor complex, which serves to link clathrin to receptors in coated vesicles. The encoded protein is found on the cytoplasmic face of coated vesicles in the plasma membrane. Two transcript variants encoding different isoforms have been found for this gene.[3]
Interactions
AP2B1 has been shown to interact with:
- AP1M2,[4]
- Arrestin beta 2,[5][6]
- BUB1B,[7]
- LDLRAP1[4][8] and
- TGF beta receptor 2.[9]
References
- ↑ "The beta 1 and beta 2 subunits of the AP complexes are the clathrin coat assembly components". The EMBO Journal 12 (13): 5237–44. Dec 1993. doi:10.1002/j.1460-2075.1993.tb06219.x. PMID 8262066.
- ↑ "Chromosome localization of human genes for clathrin adaptor polypeptides AP2 beta and AP50 and the clathrin-binding protein, VCP". Genomics 30 (1): 94–7. Nov 1995. doi:10.1006/geno.1995.0016. PMID 8595912.
- ↑ 3.0 3.1 "Entrez Gene: AP2B1 adaptor-related protein complex 2, beta 1 subunit". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=163.
- ↑ 4.0 4.1 "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- ↑ "The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis". Proceedings of the National Academy of Sciences of the United States of America 96 (7): 3712–7. Mar 1999. doi:10.1073/pnas.96.7.3712. PMID 10097102. Bibcode: 1999PNAS...96.3712L.
- ↑ "Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking". The Journal of Biological Chemistry 277 (34): 30760–8. Aug 2002. doi:10.1074/jbc.M204528200. PMID 12070169.
- ↑ "The beta2-adaptin clathrin adaptor interacts with the mitotic checkpoint kinase BubR1". Biochemical and Biophysical Research Communications 298 (5): 720–30. Nov 2002. doi:10.1016/s0006-291x(02)02522-6. PMID 12419313.
- ↑ "ARH is a modular adaptor protein that interacts with the LDL receptor, clathrin, and AP-2". The Journal of Biological Chemistry 277 (46): 44044–9. Nov 2002. doi:10.1074/jbc.M208539200. PMID 12221107.
- ↑ "Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit". Molecular Biology of the Cell 13 (11): 4001–12. Nov 2002. doi:10.1091/mbc.02-07-0104. PMID 12429842.
Further reading
- "Clathrin". Annual Review of Biochemistry 69: 699–727. 2000. doi:10.1146/annurev.biochem.69.1.699. PMID 10966473.
- "Structure--function relationships in HIV-1 Nef". EMBO Reports 2 (7): 580–5. Jul 2001. doi:10.1093/embo-reports/kve141. PMID 11463741.
- "Conservation and diversity in families of coated vesicle adaptins". The Journal of Biological Chemistry 265 (9): 4814–20. Mar 1990. doi:10.1016/S0021-9258(19)34045-1. PMID 1969413.
- "Co-localization of HIV-1 Nef with the AP-2 adaptor protein complex correlates with Nef-induced CD4 down-regulation". The EMBO Journal 16 (23): 6964–76. Dec 1997. doi:10.1093/emboj/16.23.6964. PMID 9384576.
- "ATM binds to beta-adaptin in cytoplasmic vesicles". Proceedings of the National Academy of Sciences of the United States of America 95 (17): 10146–51. Aug 1998. doi:10.1073/pnas.95.17.10146. PMID 9707615.
- "A dileucine motif in HIV-1 Nef is essential for sorting into clathrin-coated pits and for downregulation of CD4". Current Biology 8 (22): 1239–42. Nov 1998. doi:10.1016/S0960-9822(07)00518-0. PMID 9811611.
- "Interactions of the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes modulate intracellular and cell surface expression of envelope glycoproteins". Journal of Virology 73 (2): 1350–61. Feb 1999. doi:10.1128/JVI.73.2.1350-1361.1999. PMID 9882340.
- "The structure and function of the beta 2-adaptin appendage domain". The EMBO Journal 19 (16): 4216–27. Aug 2000. doi:10.1093/emboj/19.16.4216. PMID 10944104.
- "Identification of a motif in the carboxyl terminus of CXCR2 that is involved in adaptin 2 binding and receptor internalization". Biochemistry 40 (3): 791–800. Jan 2001. doi:10.1021/bi001661b. PMID 11170396.
- "Mechanism for down-regulation of CD28 by Nef". The EMBO Journal 20 (7): 1593–604. Apr 2001. doi:10.1093/emboj/20.7.1593. PMID 11285224.
- "beta-Arrestin/AP-2 interaction in G protein-coupled receptor internalization: identification of a beta-arrestin binging site in beta 2-adaptin". The Journal of Biological Chemistry 277 (11): 9247–54. Mar 2002. doi:10.1074/jbc.M108490200. PMID 11777907.
- "Molecular architecture and functional model of the endocytic AP2 complex". Cell 109 (4): 523–35. May 2002. doi:10.1016/S0092-8674(02)00735-3. PMID 12086608.
- "ARH is a modular adaptor protein that interacts with the LDL receptor, clathrin, and AP-2". The Journal of Biological Chemistry 277 (46): 44044–9. Nov 2002. doi:10.1074/jbc.M208539200. PMID 12221107.
- "The beta2-adaptin clathrin adaptor interacts with the mitotic checkpoint kinase BubR1". Biochemical and Biophysical Research Communications 298 (5): 720–30. Nov 2002. doi:10.1016/S0006-291X(02)02522-6. PMID 12419313.
- "Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit". Molecular Biology of the Cell 13 (11): 4001–12. Nov 2002. doi:10.1091/mbc.02-07-0104. PMID 12429842.
- "Clint: a novel clathrin-binding ENTH-domain protein at the Golgi". Molecular Biology of the Cell 13 (11): 4060–73. Nov 2002. doi:10.1091/mbc.E02-03-0171. PMID 12429846.
External links
- Human AP2B1 genome location and AP2B1 gene details page in the UCSC Genome Browser.
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