AP2B1

Adaptor-related protein complex 2, beta 1 subunit

PDB rendering based on 1e42.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1E42, 2G30, 2IV8, 2IV9, 2JKR, 2JKT, 2VGL, 2XA7, 4UQI

Identifiers

Symbols

AP2B1 ; ADTB2; AP105B; AP2-BETA; CLAPB1

External IDs

OMIM: 601025 MGI: 1919020 HomoloGene: 68176 GeneCards: AP2B1 Gene

Gene ontology
Molecular function	• signal sequence binding • protein binding • protein transporter activity • clathrin binding • protein complex binding • clathrin adaptor activity
Cellular component	• trans-Golgi network • cytosol • plasma membrane • membrane • AP-2 adaptor complex • endocytic vesicle membrane • clathrin-coated endocytic vesicle membrane • intracellular membrane-bounded organelle
Biological process	• intracellular protein transport • epidermal growth factor receptor signaling pathway • synaptic transmission • axon guidance • viral process • antigen processing and presentation of exogenous peptide antigen via MHC class II • negative regulation of epidermal growth factor receptor signaling pathway • neurotrophin TRK receptor signaling pathway • ephrin receptor signaling pathway • clathrin coat assembly • regulation of defense response to virus by virus • clathrin-mediated endocytosis
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

163

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 17:
35.58 – 35.73 Mb

Chr 11:
83.3 – 83.41 Mb

PubMed search

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 assembly protein complex 2, 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:

References

↑ Gallusser A, Kirchhausen T (Dec 1993). "The beta 1 and beta 2 subunits of the AP complexes are the clathrin coat assembly components". The EMBO Journal 12 (13): 5237–44. PMC 413789. PMID 8262066.
↑ Druck T, Gu Y, Prabhala G, Cannizzaro LA, Park SH, Huebner K, Keen JH (Nov 1995). "Chromosome localization of human genes for clathrin adaptor polypeptides AP2 beta and AP50 and the clathrin-binding protein, VCP". Genomics 30 (1): 94–7. doi:10.1006/geno.1995.0016. PMID 8595912.
1 2 "Entrez Gene: AP2B1 adaptor-related protein complex 2, beta 1 subunit".
1 2 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 (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
↑ Laporte SA, Oakley RH, Zhang J, Holt JA, Ferguson SS, Caron MG, Barak LS (Mar 1999). "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. doi:10.1073/pnas.96.7.3712. PMC 22359. PMID 10097102.
↑ Kim YM, Benovic JL (Aug 2002). "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. doi:10.1074/jbc.M204528200. PMID 12070169.
↑ Cayrol C, Cougoule C, Wright M (Nov 2002). "The beta2-adaptin clathrin adaptor interacts with the mitotic checkpoint kinase BubR1". Biochemical and Biophysical Research Communications 298 (5): 720–30. doi:10.1016/s0006-291x(02)02522-6. PMID 12419313.
↑ He G, Gupta S, Yi M, Michaely P, Hobbs HH, Cohen JC (Nov 2002). "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. doi:10.1074/jbc.M208539200. PMID 12221107.
↑ Yao D, Ehrlich M, Henis YI, Leof EB (Nov 2002). "Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit". Molecular Biology of the Cell 13 (11): 4001–12. doi:10.1091/mbc.02-07-0104. PMC 133610. PMID 12429842.

Kirchhausen T (2000). "Clathrin". Annual Review of Biochemistry 69: 699–727. doi:10.1146/annurev.biochem.69.1.699. PMID 10966473.
Geyer M, Fackler OT, Peterlin BM (Jul 2001). "Structure--function relationships in HIV-1 Nef". EMBO Reports 2 (7): 580–5. doi:10.1093/embo-reports/kve141. PMC 1083955. PMID 11463741.
Ponnambalam S, Robinson MS, Jackson AP, Peiperl L, Parham P (Mar 1990). "Conservation and diversity in families of coated vesicle adaptins". The Journal of Biological Chemistry 265 (9): 4814–20. PMID 1969413.
Greenberg ME, Bronson S, Lock M, Neumann M, Pavlakis GN, Skowronski J (Dec 1997). "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. doi:10.1093/emboj/16.23.6964. PMC 1170300. PMID 9384576.
Lim DS, Kirsch DG, Canman CE, Ahn JH, Ziv Y, Newman LS, Darnell RB, Shiloh Y, Kastan MB (Aug 1998). "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. doi:10.1073/pnas.95.17.10146. PMC 21476. PMID 9707615.
Greenberg M, DeTulleo L, Rapoport I, Skowronski J, Kirchhausen T (Nov 1998). "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. doi:10.1016/S0960-9822(07)00518-0. PMID 9811611.
Berlioz-Torrent C, Shacklett BL, Erdtmann L, Delamarre L, Bouchaert I, Sonigo P, Dokhelar MC, Benarous R (Feb 1999). "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. PMC 103959. PMID 9882340.
Owen DJ, Vallis Y, Pearse BM, McMahon HT, Evans PR (Aug 2000). "The structure and function of the beta 2-adaptin appendage domain". The EMBO Journal 19 (16): 4216–27. doi:10.1093/emboj/19.16.4216. PMC 302036. PMID 10944104.
Fan GH, Yang W, Wang XJ, Qian Q, Richmond A (Jan 2001). "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. doi:10.1021/bi001661b. PMC 2664867. PMID 11170396.
Swigut T, Shohdy N, Skowronski J (Apr 2001). "Mechanism for down-regulation of CD28 by Nef". The EMBO Journal 20 (7): 1593–604. doi:10.1093/emboj/20.7.1593. PMC 145469. PMID 11285224.
Laporte SA, Miller WE, Kim KM, Caron MG (Mar 2002). "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. doi:10.1074/jbc.M108490200. PMID 11777907.
Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ (May 2002). "Molecular architecture and functional model of the endocytic AP2 complex". Cell 109 (4): 523–35. doi:10.1016/S0092-8674(02)00735-3. PMID 12086608.
He G, Gupta S, Yi M, Michaely P, Hobbs HH, Cohen JC (Nov 2002). "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. doi:10.1074/jbc.M208539200. PMID 12221107.
Cayrol C, Cougoule C, Wright M (Nov 2002). "The beta2-adaptin clathrin adaptor interacts with the mitotic checkpoint kinase BubR1". Biochemical and Biophysical Research Communications 298 (5): 720–30. doi:10.1016/S0006-291X(02)02522-6. PMID 12419313.
Yao D, Ehrlich M, Henis YI, Leof EB (Nov 2002). "Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit". Molecular Biology of the Cell 13 (11): 4001–12. doi:10.1091/mbc.02-07-0104. PMC 133610. PMID 12429842.
Kalthoff C, Groos S, Kohl R, Mahrhold S, Ungewickell EJ (Nov 2002). "Clint: a novel clathrin-binding ENTH-domain protein at the Golgi". Molecular Biology of the Cell 13 (11): 4060–73. doi:10.1091/mbc.E02-03-0171. PMC 133614. PMID 12429846.

PDB gallery

1e42: BETA2-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2

1gw5:

1w63: AP1 CLATHRIN ADAPTOR CORE

2g30: beta appendage of AP2 complexed with ARH peptide

2iv9: B2-APPENDAGE FROM AP2 IN COMPLEX WITH EPS15 PEPTIDE

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AP2B1

Function

Interactions

References

Further reading