VPS24

CHMP3

Available structures

Ortholog search: PDBe RCSB

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

Identifiers

Aliases

CHMP3, NEDF, VPS24, CGI-149, charged multivesicular body protein 3

External IDs

MGI: 1913950 HomoloGene: 6368 GeneCards: CHMP3

Gene ontology
Molecular function	• protein binding • phosphatidylcholine binding • protein homodimerization activity • ubiquitin-specific protease binding
Cellular component	• cytoplasm • cytoplasmic, membrane-bounded vesicle • membrane • plasma membrane • endosome • late endosome membrane • extracellular exosome • ESCRT III complex • cytosol
Biological process	• autophagosome maturation • viral life cycle • protein polymerization • multivesicular body assembly • cell cycle • cell division • regulation of mitotic spindle assembly • endosomal transport • regulation of centrosome duplication • apoptotic process • protein heterooligomerization • negative regulation of viral release from host cell • regulation of viral process • autophagy • vacuolar transport • cell separation after cytokinesis • transport • protein transport • nucleus organization • mitotic metaphase plate congression • multivesicular body sorting pathway • regulation of exosomal secretion • viral budding via host ESCRT complex • positive regulation of viral release from host cell
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


51652


66700

Ensembl


ENSG00000115561


ENSMUSG00000053119

UniProt


Q9Y3E7


Q9CQ10

RefSeq (mRNA)


NM_001005753 NM_001193517 NM_016079


NM_025783

RefSeq (protein)


NP_001005753.1 NP_001180446.1 NP_001185883.1 NP_057163.1


NP_080059.2

Location (UCSC)

Chr 2: 86.5 – 86.56 Mb

Chr 6: 71.54 – 71.58 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Charged multivesicular body protein 3 is a protein that in humans is encoded by the VPS24 gene.^[3]^[4]^[5]

Function

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.^[5]

Interactions

VPS24 has been shown to interact with IGFBP7.^[3]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 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.
1 2 "Entrez Gene: VPS24 vacuolar protein sorting 24 homolog (S. cerevisiae)".

Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W (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, Meerloo T, Emr SD (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.
Su ZZ, Kang DC, Chen Y, Pekarskaya O, Chao W, Volsky DJ, Fisher PB (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:10.1080/13550280390201263. PMID 12775420.
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.
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.
Martin-Serrano J, Yarovoy A, Perez-Caballero D, Bieniasz PD, Yaravoy A (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, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional Proteomics Mapping of a Human Signaling Pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
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.
Yan Q, Hunt PR, Frelin L, Vida TA, Pevsner J, Bean AJ (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.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (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, Paisley TE, Oh Y (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, Slagsvold T, Raiborg C, Lechardeur D, Wälchli S, Lukacs GL, Brech A, Stenmark H (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, 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.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (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, Popova E, Palu G, Göttlinger H (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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VPS24

Function

Interactions

References

Further reading