AP1S1

Adaptor-related protein complex 1, sigma 1 subunit

Rendering of AP1S1 from PDB 1w63

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
4P6Z

Identifiers

Symbols

AP1S1 ; AP19; CLAPS1; EKV3; MEDNIK; SIGMA1A

External IDs

OMIM: 603531 MGI: 1098244 HomoloGene: 20342 GeneCards: AP1S1 Gene

Gene ontology
Molecular function	• protein transporter activity
Cellular component	• Golgi membrane • lysosomal membrane • cytosol • coated pit • membrane • AP-1 adaptor complex • cytoplasmic vesicle membrane • clathrin-coated endocytic vesicle membrane • trans-Golgi network membrane • extracellular exosome
Biological process	• intracellular protein transport • post-Golgi vesicle-mediated transport • receptor-mediated endocytosis • response to virus • viral process • antigen processing and presentation of exogenous peptide antigen via MHC class II • regulation of defense response to virus by virus • membrane organization
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 7:
101.15 – 101.16 Mb

Chr 5:
137.03 – 137.05 Mb

PubMed search

AP-1 complex subunit sigma-1A is a protein that in humans is encoded by the AP1S1 gene.^[1]^[2]^[3]

Function

The protein encoded by this gene is part of the clathrin coat assembly complex which links clathrin to receptors in coated vesicles. These vesicles are involved in endocytosis and Golgi processing. This protein, as well as beta-prime-adaptin, gamma-adaptin, and the medium (mu) chain AP47, form the AP-1 assembly protein complex located at the Golgi vesicle. Two alternatively spliced transcript variants of this gene, which encode distinct isoforms, have been reported.^[3]

A mutation in the AP1S1 causes the rare familial MEDNIK syndrome described in 2008.^[4]

Interactions

AP1S1 has been shown to interact with AP1G1^[2]^[5]^[6] and RAB10.^[7]

References

↑ 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.
1 2 Takatsu H, Sakurai M, Shin HW, Murakami K, Nakayama K (Sep 1998). "Identification and characterization of novel clathrin adaptor-related proteins". The Journal of Biological Chemistry 273 (38): 24693–700. doi:10.1074/jbc.273.38.24693. PMID 9733768.
1 2 "Entrez Gene: AP1S1 adaptor-related protein complex 1, sigma 1 subunit".
↑ Montpetit A, Côté S, Brustein E, Drouin CA, Lapointe L, Boudreau M, Meloche C, Drouin R, Hudson TJ, Drapeau P, Cossette P (Dec 2008). Van Heyningen V, ed. "Disruption of AP1S1, causing a novel neurocutaneous syndrome, perturbs development of the skin and spinal cord". PLoS Genetics 4 (12): e1000296. doi:10.1371/journal.pgen.1000296. PMC 2585812. PMID 19057675.
↑ 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.
↑ 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.
↑ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

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.
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.
Kirchhausen T, Davis AC, Frucht S, Greco BO, Payne GS, Tubb B (Jun 1991). "AP17 and AP19, the mammalian small chains of the clathrin-associated protein complexes show homology to Yap17p, their putative homolog in yeast". The Journal of Biological Chemistry 266 (17): 11153–7. PMID 2040623.
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. 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.
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.
"Toward a complete human genome sequence". Genome Research 8 (11): 1097–108. Nov 1998. doi:10.1101/gr.8.11.1097. PMID 9847074.
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.
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.
Wyss S, Berlioz-Torrent C, Boge M, Blot G, Höning S, Benarous R, Thali M (Mar 2001). "The highly conserved C-terminal dileucine motif in the cytosolic domain of the human immunodeficiency virus type 1 envelope glycoprotein is critical for its association with the AP-1 clathrin adaptor [correction of adapter]". Journal of Virology 75 (6): 2982–92. doi:10.1128/JVI.75.6.2982-2992.2001. PMC 115924. PMID 11222723.
Boehm M, Aguilar RC, Bonifacino JS (Nov 2001). "Functional and physical interactions of the adaptor protein complex AP-4 with ADP-ribosylation factors (ARFs)". The EMBO Journal 20 (22): 6265–76. doi:10.1093/emboj/20.22.6265. PMC 125733. PMID 11707398.
Janvier K, Craig H, Hitchin D, Madrid R, Sol-Foulon N, Renault L, Cherfils J, Cassel D, Benichou S, Guatelli J (Mar 2003). "HIV-1 Nef stabilizes the association of adaptor protein complexes with membranes". The Journal of Biological Chemistry 278 (10): 8725–32. doi:10.1074/jbc.M210115200. PMID 12486136.

PDB gallery

1w63: AP1 CLATHRIN ADAPTOR CORE

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AP1S1

Function

Interactions

References

Further reading