AP1M1
AP-1 complex subunit mu-1 is a protein that in humans is encoded by the AP1M1 gene.[5][6]
Function
The protein encoded by this gene is the medium chain of the trans-Golgi network clathrin-associated protein complex AP-1. The other components of this complex are beta-prime-adaptin, gamma-adaptin, and the small chain AP1S1. This complex is located at the Golgi vesicle and links clathrin to receptors in coated vesicles. These vesicles are involved in endocytosis and Golgi processing.[7]
References
- GRCh38: Ensembl release 89: ENSG00000072958 - Ensembl, May 2017
- GRCm38: Ensembl release 89: ENSMUSG00000003033 - Ensembl, May 2017
- "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- Peyrard M, Parveneh S, Lagercrantz S, Ekman M, Fransson I, Sahlén S, Dumanski JP (Jun 1998). "Cloning, expression pattern, and chromosomal assignment to 16q23 of the human gamma-adaptin gene (ADTG)". Genomics. 50 (2): 275–80. doi:10.1006/geno.1998.5289. PMID 9653655.
- Medigeshi GR, Krikunova M, Radhakrishnan K, Wenzel D, Klingauf J, Schu P (Jan 2008). "AP-1 membrane-cytoplasm recycling regulated by mu1A-adaptin". Traffic. 9 (1): 121–32. doi:10.1111/j.1600-0854.2007.00672.x. PMID 17988225.
- "Entrez Gene: AP1M1 adaptor-related protein complex 1, mu 1 subunit".
- Hinners I, Wendler F, Fei H, Thomas L, Thomas G, Tooze SA (Dec 2003). "AP-1 recruitment to VAMP4 is modulated by phosphorylation-dependent binding of PACS-1". EMBO Reports. 4 (12): 1182–9. doi:10.1038/sj.embor.7400018. PMC 1326413. PMID 14608369.
- Fölsch H, Ohno H, Bonifacino JS, Mellman I (Oct 1999). "A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells". Cell. 99 (2): 189–98. doi:10.1016/S0092-8674(00)81650-5. PMID 10535737. S2CID 15288582.
- Page LJ, Robinson MS (Nov 1995). "Targeting signals and subunit interactions in coated vesicle adaptor complexes". The Journal of Cell Biology. 131 (3): 619–30. doi:10.1083/jcb.131.3.619. PMC 2120623. PMID 7593184.
Further reading
- 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.
- Bénichou S, Benmerah A (Jan 2003). "[The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites"of the endocytosis pathway]". Médecine/Sciences. 19 (1): 100–6. doi:10.1051/medsci/2003191100. PMID 12836198.
- Ohno H, Stewart J, Fournier MC, Bosshart H, Rhee I, Miyatake S, Saito T, Gallusser A, Kirchhausen T, Bonifacino JS (Sep 1995). "Interaction of tyrosine-based sorting signals with clathrin-associated proteins". Science. 269 (5232): 1872–5. Bibcode:1995Sci...269.1872O. doi:10.1126/science.7569928. PMID 7569928.
- Page LJ, Robinson MS (Nov 1995). "Targeting signals and subunit interactions in coated vesicle adaptor complexes". The Journal of Cell Biology. 131 (3): 619–30. doi:10.1083/jcb.131.3.619. PMC 2120623. PMID 7593184.
- Seaman MN, Sowerby PJ, Robinson MS (Oct 1996). "Cytosolic and membrane-associated proteins involved in the recruitment of AP-1 adaptors onto the trans-Golgi network". The Journal of Biological Chemistry. 271 (41): 25446–51. doi:10.1074/jbc.271.41.25446. PMID 8810314.
- Mangasarian A, Foti M, Aiken C, Chin D, Carpentier JL, Trono D (Jan 1997). "The HIV-1 Nef protein acts as a connector with sorting pathways in the Golgi and at the plasma membrane". Immunity. 6 (1): 67–77. doi:10.1016/S1074-7613(00)80243-5. PMID 9052838.
- Foti M, Mangasarian A, Piguet V, Lew DP, Krause KH, Trono D, Carpentier JL (Oct 1997). "Nef-mediated clathrin-coated pit formation". The Journal of Cell Biology. 139 (1): 37–47. doi:10.1083/jcb.139.1.37. PMC 2139808. PMID 9314527.
- Ohno H, Aguilar RC, Fournier MC, Hennecke S, Cosson P, Bonifacino JS (Nov 1997). "Interaction of endocytic signals from the HIV-1 envelope glycoprotein complex with members of the adaptor medium chain family". Virology. 238 (2): 305–15. doi:10.1006/viro.1997.8839. PMID 9400603.
- Piguet V, Chen YL, Mangasarian A, Foti M, Carpentier JL, Trono D (May 1998). "Mechanism of Nef-induced CD4 endocytosis: Nef connects CD4 with the mu chain of adaptor complexes". The EMBO Journal. 17 (9): 2472–81. doi:10.1093/emboj/17.9.2472. PMC 1170589. PMID 9564030.
- Le Gall S, Erdtmann L, Benichou S, Berlioz-Torrent C, Liu L, Benarous R, Heard JM, Schwartz O (Apr 1998). "Nef interacts with the mu subunit of clathrin adaptor complexes and reveals a cryptic sorting signal in MHC I molecules". Immunity. 8 (4): 483–95. doi:10.1016/S1074-7613(00)80553-1. PMID 9586638.
- Craig HM, Pandori MW, Guatelli JC (Sep 1998). "Interaction of HIV-1 Nef with the cellular dileucine-based sorting pathway is required for CD4 down-regulation and optimal viral infectivity". Proceedings of the National Academy of Sciences of the United States of America. 95 (19): 11229–34. Bibcode:1998PNAS...9511229C. doi:10.1073/pnas.95.19.11229. PMC 21624. PMID 9736718.
- Bresnahan PA, Yonemoto W, Ferrell S, Williams-Herman D, Geleziunas R, Greene WC (Nov 1998). "A dileucine motif in HIV-1 Nef acts as an internalization signal for CD4 downregulation and binds the AP-1 clathrin adaptor". Current Biology. 8 (22): 1235–8. doi:10.1016/S0960-9822(07)00517-9. PMID 9811606. S2CID 16541580.
- 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. S2CID 14272751.
- Owen DJ, Evans PR (Nov 1998). "A structural explanation for the recognition of tyrosine-based endocytotic signals". Science. 282 (5392): 1327–32. Bibcode:1998Sci...282.1327O. doi:10.1126/science.282.5392.1327. PMC 5600252. PMID 9812899.
- 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. doi:10.1128/JVI.73.2.1350-1361.1999. PMC 103959. PMID 9882340.
- Fölsch H, Ohno H, Bonifacino JS, Mellman I (Oct 1999). "A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells". Cell. 99 (2): 189–98. doi:10.1016/S0092-8674(00)81650-5. PMID 10535737. S2CID 15288582.
- Orzech E, Cohen S, Weiss A, Aroeti B (May 2000). "Interactions between the exocytic and endocytic pathways in polarized Madin-Darby canine kidney cells". The Journal of Biological Chemistry. 275 (20): 15207–19. doi:10.1074/jbc.275.20.15207. PMID 10809756.
- Umeda A, Meyerholz A, Ungewickell E (May 2000). "Identification of the universal cofactor (auxilin 2) in clathrin coat dissociation". European Journal of Cell Biology. 79 (5): 336–42. doi:10.1078/S0171-9335(04)70037-0. PMID 10887964.
- Nakagawa T, Setou M, Seog D, Ogasawara K, Dohmae N, Takio K, Hirokawa N (Nov 2000). "A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex". Cell. 103 (4): 569–81. doi:10.1016/S0092-8674(00)00161-6. PMID 11106728. S2CID 18245989.
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