Biology:AP1B1
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
AP-1 complex subunit beta-1 is a protein that in humans is encoded by the AP1B1 gene.[1][2][3]
Adaptor protein complex 1 is found at the cytoplasmic face of coated vesicles located at the Golgi complex, where it mediates both the recruitment of clathrin to the membrane and the recognition of sorting signals within the cytosolic tails of transmembrane receptors. This complex is a heterotetramer composed of two large, one medium, and one small adaptin subunit. The protein encoded by this gene serves as one of the large subunits of this complex and is a member of the adaptin protein family. This gene is a candidate meningioma gene. Two transcript variants encoding different isoforms have been found for this gene, and variants utilizing alternative polyadenylation signals exist.[3]
Interactions
AP1B1 has been shown to interact with KIF13A[4] and AP1G1.[5][6][7]
References
- ↑ "Characterization of a new member of the human beta-adaptin gene family from chromosome 22q12, a candidate meningioma gene". Hum Mol Genet 3 (8): 1393–9. January 1995. doi:10.1093/hmg/3.8.1393. PMID 7987321.
- ↑ "Structure of the promoter and genomic organization of the human beta'-adaptin gene (BAM22) from chromosome 22q12". Genomics 36 (1): 112–7. February 1997. doi:10.1006/geno.1996.0431. PMID 8812422.
- ↑ 3.0 3.1 "Entrez Gene: AP1B1 adaptor-related protein complex 1, beta 1 subunit". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=162.
- ↑ Nakagawa, T; Setou M; Seog D; Ogasawara K; Dohmae N; Takio K; Hirokawa N (November 2000). "A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex". Cell (UNITED STATES) 103 (4): 569–81. doi:10.1016/S0092-8674(00)00161-6. ISSN 0092-8674. PMID 11106728.
- ↑ Takatsu, H; Sakurai M; Shin H W; Murakami K; Nakayama K (September 1998). "Identification and characterization of novel clathrin adaptor-related proteins". J. Biol. Chem. (UNITED STATES) 273 (38): 24693–700. doi:10.1074/jbc.273.38.24693. ISSN 0021-9258. PMID 9733768.
- ↑ Fölsch, H; Ohno H; Bonifacino J S; Mellman I (October 1999). "A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells". Cell (UNITED STATES) 99 (2): 189–98. doi:10.1016/S0092-8674(00)81650-5. ISSN 0092-8674. PMID 10535737.
- ↑ Page, L J; Robinson M S (November 1995). "Targeting signals and subunit interactions in coated vesicle adaptor complexes". J. Cell Biol. (UNITED STATES) 131 (3): 619–30. doi:10.1083/jcb.131.3.619. ISSN 0021-9525. PMID 7593184.
Further reading
- Kirchhausen T (2000). "Clathrin.". Annu. Rev. Biochem. 69: 699–727. doi:10.1146/annurev.biochem.69.1.699. PMID 10966473.
- "Structure--function relationships in HIV-1 Nef.". EMBO Rep. 2 (7): 580–5. 2001. doi:10.1093/embo-reports/kve141. PMID 11463741.
- "[The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites"of the endocytosis pathway]". Med Sci (Paris) 19 (1): 100–6. 2003. doi:10.1051/medsci/2003191100. PMID 12836198.
- "ATM binds to beta-adaptin in cytoplasmic vesicles.". Proc. Natl. Acad. Sci. U.S.A. 95 (17): 10146–51. 1998. doi:10.1073/pnas.95.17.10146. PMID 9707615. Bibcode: 1998PNAS...9510146L.
- "Identification and characterization of novel clathrin adaptor-related proteins.". J. Biol. Chem. 273 (38): 24693–700. 1998. doi:10.1074/jbc.273.38.24693. PMID 9733768.
- "Interaction of HIV-1 Nef with the cellular dileucine-based sorting pathway is required for CD4 down-regulation and optimal viral infectivity.". Proc. Natl. Acad. Sci. U.S.A. 95 (19): 11229–34. 1998. doi:10.1073/pnas.95.19.11229. PMID 9736718. Bibcode: 1998PNAS...9511229C.
- "A dileucine motif in HIV-1 Nef acts as an internalization signal for CD4 downregulation and binds the AP-1 clathrin adaptor.". Curr. Biol. 8 (22): 1235–8. 1999. doi:10.1016/S0960-9822(07)00517-9. PMID 9811606.
- "A dileucine motif in HIV-1 Nef is essential for sorting into clathrin-coated pits and for downregulation of CD4.". Curr. Biol. 8 (22): 1239–42. 1999. doi:10.1016/S0960-9822(07)00518-0. PMID 9811611.
- "The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis.". Proc. Natl. Acad. Sci. U.S.A. 96 (7): 3712–7. 1999. doi:10.1073/pnas.96.7.3712. PMID 10097102. Bibcode: 1999PNAS...96.3712L.
- "A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells.". Cell 99 (2): 189–98. 1999. doi:10.1016/S0092-8674(00)81650-5. PMID 10535737.
- "Substrate specificities and identification of putative substrates of ATM kinase family members.". J. Biol. Chem. 274 (53): 37538–43. 2000. doi:10.1074/jbc.274.53.37538. PMID 10608806.
- "The calcineurin-binding protein cain is a negative regulator of synaptic vesicle endocytosis.". J. Biol. Chem. 275 (44): 34017–20. 2000. doi:10.1074/jbc.C000429200. PMID 10931822.
- "A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex.". Cell 103 (4): 569–81. 2001. doi:10.1016/S0092-8674(00)00161-6. PMID 11106728.
- "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using yeast three-hybrid system.". Biochem. Biophys. Res. Commun. 284 (4): 1083–9. 2001. doi:10.1006/bbrc.2001.5081. PMID 11409905.
- "Gamma subunit of the AP-1 adaptor complex binds clathrin: implications for cooperative binding in coated vesicle assembly.". Mol. Biol. Cell 12 (7): 1925–35. 2001. doi:10.1091/mbc.12.7.1925. PMID 11451993.
- "Molecular mechanism of transforming growth factor (TGF)-beta1-induced glutathione depletion in alveolar epithelial cells. Involvement of AP-1/ARE and Fra-1.". J. Biol. Chem. 277 (24): 21158–66. 2002. doi:10.1074/jbc.M112145200. PMID 11912197.
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External links
- Human AP1B1 genome location and AP1B1 gene details page in the UCSC Genome Browser.
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