VPS24

From Wikipedia, the free encyclopedia

Charged multivesicular body protein 3

PDB rendering based on 2gd5.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2GD5, 2XZE, 3FRT, 3FRV

Identifiers

CHMP3; NEDF; VPS24

External IDs

OMIM: 610052 MGI: 1913950 HomoloGene: 6368 GeneCards: CHMP3 Gene

Gene Ontology
Molecular function	• protein binding
Cellular component	• cytosol • late endosome membrane
Biological process	• apoptotic process • cell cycle • protein transport • cellular membrane organization • endosomal transport • cell division
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000115561

ENSMUSG00000053119

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
86.73 – 86.95 Mb

Chr 6:
71.54 – 71.58 Mb

PubMed search

Charged multivesicular body protein 3 is a protein that in humans is encoded by the VPS24 gene.^[1]^[2]^[3]

This gene encodes a protein that acts in the sorting of transmembrane proteins into lysosomes/vacuoles via the multivesicular body (MVB) pathway. This protein, along with other soluble coiled-coil containing proteins, forms part of the ESCRT-III protein complex that binds to the endosomal membrane and recruits additional cofactors for protein sorting into the MVB. This protein may also co-immunoprecipitate with a member of the IFG-binding protein superfamily. Alternative splicing results in multiple transcript variants encoding different isoforms.^[3]

Interactions

VPS24 has been shown to interact with IGFBP7.^[1]

References

↑ 1.0 1.1 Wilson EM, Oh Y, Hwa V, Rosenfeld RG (Sep 2001). "Interaction of IGF-binding protein-related protein 1 with a novel protein, neuroendocrine differentiation factor, results in neuroendocrine differentiation of prostate cancer cells". J Clin Endocrinol Metab 86 (9): 4504–11. doi:10.1210/jc.86.9.4504. PMID 11549700.
↑ Whitley P, Reaves BJ, Hashimoto M, Riley AM, Potter BV, Holman GD (Sep 2003). "Identification of mammalian Vps24p as an effector of phosphatidylinositol 3,5-bisphosphate-dependent endosome compartmentalization". J Biol Chem 278 (40): 38786–95. doi:10.1074/jbc.M306864200. PMID 12878588.
↑ 3.0 3.1 "Entrez Gene: VPS24 vacuolar protein sorting 24 homolog (S. cerevisiae)".

Further reading

Lai CH, Chou CY, Ch'ang LY et al. (2000). "Identification of Novel Human Genes Evolutionarily Conserved in Caenorhabditis elegans by Comparative Proteomics". Genome Res. 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093.
Babst M, Katzmann DJ, Estepa-Sabal EJ et al. (2002). "Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting". Dev. Cell 3 (2): 271–82. doi:10.1016/S1534-5807(02)00220-4. PMID 12194857.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Su ZZ, Kang DC, Chen Y et al. (2003). "Identification of gene products suppressed by human immunodeficiency virus type 1 infection or gp120 exposure of primary human astrocytes by rapid subtraction hybridization". J. Neurovirol. 9 (3): 372–89. doi:10.1080/713831538. PMID 12775420.
Strack B, Calistri A, Craig S et al. (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.
von Schwedler UK, Stuchell M, Müller B et al. (2003). "The protein network of HIV budding". Cell 114 (6): 701–13. doi:10.1016/S0092-8674(03)00714-1. PMID 14505570.
Martin-Serrano J, Yarovoy A, Perez-Caballero D et al. (2003). "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins". Proc. Natl. Acad. Sci. U.S.A. 100 (21): 12414–9. doi:10.1073/pnas.2133846100. PMC 218772. PMID 14519844.
Colland F, Jacq X, Trouplin V et al. (2004). "Functional Proteomics Mapping of a Human Signaling Pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Lin Y, Kimpler LA, Naismith TV et al. (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.
Yan Q, Hunt PR, Frelin L et al. (2005). "mVps24p functions in EGF receptor sorting/trafficking from the early endosome". Exp. Cell Res. 304 (1): 265–73. doi:10.1016/j.yexcr.2004.11.003. PMID 15707591.
Hillier LW, Graves TA, Fulton RS et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.
Rual JF, Venkatesan K, Hao T et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Walker GE, Antoniono RJ, Ross HJ et al. (2006). "Neuroendocrine-like differentiation of non-small cell lung carcinoma cells: regulation by cAMP and the interaction of mac25/IGFBP-rP1 and 25.1". Oncogene 25 (13): 1943–54. doi:10.1038/sj.onc.1209213. PMID 16302002.
Bache KG, Stuffers S, Malerød L et al. (2006). "The ESCRT-III Subunit hVps24 Is Required for Degradation but Not Silencing of the Epidermal Growth Factor Receptor". Mol. Biol. Cell 17 (6): 2513–23. doi:10.1091/mbc.E05-10-0915. PMC 1474783. PMID 16554368.
Tsang HT, Connell JW, Brown SE et al. (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.
Olsen JV, Blagoev B, Gnad F et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
Zamborlini A, Usami Y, Radoshitzky SR et al. (2007). "Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding". Proc. Natl. Acad. Sci. U.S.A. 103 (50): 19140–5. doi:10.1073/pnas.0603788103. PMC 1748189. PMID 17146056.

PDB gallery

2gd5: Structural basis for budding by the ESCRTIII factor CHMP3

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