AP1M1

AP1M1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1W63, 4EMZ, 4EN2, 4HMY, 4P6Z
Identifiers
Aliases	AP1M1 , AP47, CLAPM2, CLTNM, MU-1A, adaptor related protein complex 1 mu 1 subunit, adaptor related protein complex 1 subunit mu 1, mu1A
External IDs	OMIM: 603535; MGI: 102776; HomoloGene: 4017; GeneCards: AP1M1; OMA:AP1M1 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) [1] Band 19p13.11 Start 16,197,854 bp [1] End 16,245,906 bp [1]
Gene location (Mouse) Chr. Chromosome 8 (mouse) [2] Band 8 B3.3|8 34.92 cM Start 72,993,862 bp [2] End 73,011,229 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte right lobe of liver left testis right testis stromal cell of endometrium prefrontal cortex mucosa of ileum monocyte ganglionic eminence right coronary artery Top expressed in seminiferous tubule internal carotid artery external carotid artery granulocyte facial motor nucleus endothelial cell of lymphatic vessel neural layer of retina Rostral migratory stream ganglionic eminence vas deferens More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding Cellular component cytosol clathrin-coated endocytic vesicle membrane Golgi apparatus trans-Golgi network membrane membrane Golgi membrane lysosomal membrane clathrin-coated vesicle membrane extracellular exosome cytoplasmic vesicle membrane cytoplasmic vesicle clathrin adaptor complex plasma membrane specific granule membrane Biological process antigen processing and presentation of exogenous peptide antigen via MHC class II mitigation of host defenses by virus melanosome organization endosome to melanosome transport protein transport intracellular protein transport vesicle-mediated transport viral process neutrophil degranulation transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8907 11767 Ensembl ENSG00000072958 ENSMUSG00000003033 UniProt Q9BXS5 P35585 RefSeq (mRNA) NM_001130524 NM_032493 NM_007456 RefSeq (protein) NP_001123996 NP_115882 NP_031482 Location (UCSC) Chr 19: 16.2 – 16.25 Mb Chr 8: 72.99 – 73.01 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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]

Interactions

AP1M1 has been shown to interact with VAMP4 ^[8] and AP1G1. ^{[9] [10]}

References

1. GRCh38: Ensembl release 89: ENSG00000072958 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000003033 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "Entrez Gene: AP1M1 adaptor-related protein complex 1, mu 1 subunit".
8. 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.
9. 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.
10. 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. Bibcode:1998CBio....8.1235B. 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. Bibcode:1998CBio....8.1239G. 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.

External links

• Human AP1M1 genome location and AP1M1 gene details page in the UCSC Genome Browser .