VPS4A

VPS4A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1YXR, 2JQ9, 2K3W
Identifiers
Aliases	VPS4A, SKD1, SKD1A, SKD2, VPS4, VPS4-1, vacuolar protein sorting 4 homolog A, CIMDAG
External IDs	OMIM: 609982; MGI: 1890520; HomoloGene: 69132; GeneCards: VPS4A; OMA:VPS4A - orthologs
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16q22.1 Start 69,311,350 bp[1] End 69,326,939 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8|8 D3 Start 107,757,854 bp[2] End 107,772,387 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastrocnemius muscle cerebellar vermis muscle of thigh Skeletal muscle tissue of rectus abdominis parotid gland apex of heart Brodmann area 23 middle temporal gyrus right frontal lobe endothelial cell Top expressed in spermatid spermatocyte seminiferous tubule neural layer of retina dentate gyrus of hippocampal formation granule cell dorsal tegmental nucleus superior colliculus pontine nuclei medial dorsal nucleus primary visual cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding protein domain specific binding microtubule-severing ATPase activity protein C-terminus binding protein binding hydrolase activity ATP binding ATPase activity protein-containing complex binding Cellular component cytoplasm ESCRT III complex cytosol endosome late endosome centrosome spindle pole vacuolar membrane late endosome membrane Flemming body membrane plasma membrane midbody early endosome perinuclear region of cytoplasm lysosome extracellular exosome nucleus endosome membrane Biological process late endosomal microautophagy endosomal vesicle fusion viral release from host cell abscission viral budding via host ESCRT complex nucleus organization viral life cycle multivesicular body assembly vacuole organization vesicle uncoating regulation of protein localization cell division intracellular cholesterol transport ESCRT complex disassembly vesicle budding from membrane ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway transport protein transport positive regulation of viral life cycle ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway cell cycle negative regulation of cytokinesis septum digestion after cytokinesis mitotic metaphase plate congression positive regulation of exosomal secretion vesicle-mediated transport regulation of protein localization to plasma membrane ESCRT III complex disassembly cytoplasmic microtubule organization endosomal transport macroautophagy positive regulation of viral budding via host ESCRT complex actomyosin contractile ring contraction protein targeting to lysosome nuclear envelope organization nuclear membrane reassembly mitotic cytokinesis checkpoint signaling cytoskeleton-dependent cytokinesis midbody abscission Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 27183 116733 Ensembl ENSG00000132612 ENSMUSG00000031913 UniProt Q9UN37 Q8VEJ9 RefSeq (mRNA) NM_013245 NM_126165 RefSeq (protein) NP_037377 NP_037377.1 NP_569053 Location (UCSC) Chr 16: 69.31 – 69.33 Mb Chr 8: 107.76 – 107.77 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Vacuolar protein sorting-associated protein 4A is a protein that in humans is encoded by the VPS4A gene.[5][6][7]

Function

The protein encoded by this gene is a member of the AAA protein family (ATPases associated with diverse cellular activities), and is the homolog of the yeast Vps4 protein. In humans, two paralogs of the yeast protein have been identified. They share a high degree of amino acid sequence similarity with each other, and also with yeast Vps4 and mouse proteins. Functional studies indicate that both human paralogs associate with the endosomal compartments, and are involved in intracellular protein trafficking, similar to Vps4 protein in yeast. The gene encoding this paralog has been mapped to chromosome 16; the gene for the other resides on chromosome 18.[7]

Interactions

VPS4A has been shown to interact with CHMP1A.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000132612 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031913 – 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. Bishop N, Woodman P (April 2000). "ATPase-defective Mammalian VPS4 Localizes to Aberrant Endosomes and Impairs Cholesterol Trafficking". Mol Biol Cell. 11 (1): 227–39. doi:10.1091/mbc.11.1.227. PMC 14770. PMID 10637304.
6. Scheuring S, Röhricht RA, Schöning-Burkhardt B, Beyer A, Müller S, Abts HF, Köhrer K (September 2001). "Mammalian cells express two VPS4 proteins both of which are involved in intracellular protein trafficking". J Mol Biol. 312 (3): 469–80. doi:10.1006/jmbi.2001.4917. PMID 11563910.
7. "Entrez Gene: VPS4A vacuolar protein sorting 4 homolog A (S. cerevisiae)".
8. Howard TL, Stauffer DR, Degnin CR, Hollenberg SM (July 2001). "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins". J. Cell Sci. 114 (Pt 13): 2395–404. doi:10.1242/jcs.114.13.2395. PMID 11559748.

Further reading

• Scheuring S, Bodor O, Röhricht RA, Müller S, Beyer A, Köhrer K (1999). "Cloning, characterisation, and functional expression of the Mus musculus SKD1 gene in yeast demonstrates that the mouse SKD1 and the yeast VPS4 genes are orthologues and involved in intracellular protein trafficking". Gene. 234 (1): 149–59. doi:10.1016/S0378-1119(99)00163-8. PMID 10393249.
• Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. Bibcode:2000PNAS...97.9543H. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
• Howard TL, Stauffer DR, Degnin CR, Hollenberg SM (2002). "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins". J. Cell Sci. 114 (Pt 13): 2395–404. doi:10.1242/jcs.114.13.2395. PMID 11559748.
• Tanaka H, Fujita H, Katoh H, Mori K, Negishi M (2002). "Vps4-A (vacuolar protein sorting 4-A) is a binding partner for a novel Rho family GTPase, Rnd2". Biochem. J. 365 (Pt 2): 349–53. doi:10.1042/BJ20020062. PMC 1222680. PMID 11931639.
• Nara A, Mizushima N, Yamamoto A, Kabeya Y, Ohsumi Y, Yoshimori T (2002). "SKD1 AAA ATPase-dependent endosomal transport is involved in autolysosome formation". Cell Struct. Funct. 27 (1): 29–37. doi:10.1247/csf.27.29. PMID 11937716.
• Chagnon P, Michaud J, Mitchell G, Mercier J, Marion JF, Drouin E, Rasquin-Weber A, Hudson TJ, Richter A (2003). "A Missense Mutation (R565W) in Cirhin (FLJ14728) in North American Indian Childhood Cirrhosis". Am. J. Hum. Genet. 71 (6): 1443–9. doi:10.1086/344580. PMC 378590. PMID 12417987.
• Beyer A, Scheuring S, Müller S, Mincheva A, Lichter P, Köhrer K (2003). "Comparative sequence and expression analyses of four mammalian VPS4 genes". Gene. 305 (1): 47–59. doi:10.1016/S0378-1119(02)01205-2. PMID 12594041.
• Katoh K, Shibata H, Suzuki H, Nara A, Ishidoh K, Kominami E, Yoshimori T, Maki M (2003). "The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting". J. Biol. Chem. 278 (40): 39104–13. doi:10.1074/jbc.M301604200. PMID 12860994.
• Strack B, Calistri A, Craig S, Popova E, Göttlinger HG (2003). "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding". Cell. 114 (6): 689–99. doi:10.1016/S0092-8674(03)00653-6. PMID 14505569. S2CID 10733770.
• von Schwedler UK, Stuchell M, Müller B, Ward DM, Chung HY, Morita E, Wang HE, Davis T, He GP, Cimbora DM, Scott A, Kräusslich HG, Kaplan J, Morham SG, Sundquist WI (2003). "The protein network of HIV budding". Cell. 114 (6): 701–13. doi:10.1016/S0092-8674(03)00714-1. PMID 14505570. S2CID 16894972.
• Sachse M, Strous GJ, Klumperman J (2004). "ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles". J. Cell Sci. 117 (Pt 9): 1699–708. doi:10.1242/jcs.00998. PMID 15075231.
• Lin Y, Kimpler LA, Naismith TV, Lauer JM, Hanson PI (2005). "Interaction of the mammalian endosomal sorting complex required for transport (ESCRT) III protein hSnf7-1 with itself, membranes, and the AAA+ ATPase SKD1". J. Biol. Chem. 280 (13): 12799–809. doi:10.1074/jbc.M413968200. PMID 15632132.
• Scott A, Gaspar J, Stuchell-Brereton MD, Alam SL, Skalicky JJ, Sundquist WI (2005). "Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A". Proc. Natl. Acad. Sci. U.S.A. 102 (39): 13813–8. Bibcode:2005PNAS..10213813S. doi:10.1073/pnas.0502165102. PMC 1236530. PMID 16174732.
• Tsang HT, Connell JW, Brown SE, Thompson A, Reid E, Sanderson CM (2006). "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex". Genomics. 88 (3): 333–46. doi:10.1016/j.ygeno.2006.04.003. PMID 16730941.
• Chen VY, Posada MM, Blazer LL, Zhao T, Rosania GR (2007). "The role of the VPS4A-exosome pathway in the intrinsic egress route of a DNA-binding anticancer drug". Pharm. Res. 23 (8): 1687–95. doi:10.1007/s11095-006-9043-0. PMID 16841193. S2CID 2777033.
• Lambert C, Döring T, Prange R (2007). "Hepatitis B Virus Maturation Is Sensitive to Functional Inhibition of ESCRT-III, Vps4, and γ2-Adaptin". J. Virol. 81 (17): 9050–60. doi:10.1128/JVI.00479-07. PMC 1951427. PMID 17553870.