VPS4B

Vacuolar protein sorting 4 homolog B (S. cerevisiae)

PDB rendering based on 1wr0.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1WR0, 1XWI, 2CPT, 2JQH, 2JQK

Identifiers

Symbols

VPS4B ; SKD1; SKD1B; VPS4-2

External IDs

OMIM: 609983 MGI: 1100499 HomoloGene: 37976 GeneCards: VPS4B Gene

EC number

3.6.4.6

Gene ontology
Molecular function	• protein binding • ATP binding • protein C-terminus binding • ATPase activity • ATPase activity, coupled
Cellular component	• nucleus • cytoplasm • lysosome • endosome • early endosome • late endosome • vacuolar membrane • cytosol • endosome membrane • late endosome membrane • extracellular vesicular exosome
Biological process	• ATP catabolic process • potassium ion transport • endosome organization • cell cycle • protein transport • viral process • endosomal transport • viral life cycle • intracellular cholesterol transport • endosome to lysosome transport via multivesicular body sorting pathway • response to lipid • regulation of viral process • cell division • membrane organization • positive regulation of viral release from host cell
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 18:
61.06 – 61.09 Mb

Chr 1:
106.76 – 106.8 Mb

PubMed search

Vacuolar protein sorting-associated protein 4B is a protein that in humans is encoded by the VPS4B gene.^[1]^[2]

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. The former share a high degree of aa sequence similarity with each other, and also with yeast Vps4 and mouse Skd1 proteins. Mouse Skd1 (suppressor of K+ transport defect 1) has been shown to be a yeast Vps4 ortholog. 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 18; the gene for the other resides on chromosome 16.^[2]

References

↑ Scheuring S, Rohricht RA, Schoning-Burkhardt B, Beyer A, Muller S, Abts HF, Kohrer K (Sep 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.
↑ 2.0 2.1 "Entrez Gene: VPS4B vacuolar protein sorting 4 homolog B (S. cerevisiae)".

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Mao M, Fu G, Wu JS et al. (1998). "Identification of genes expressed in human CD34+ hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 8175–80. doi:10.1073/pnas.95.14.8175. PMC 20949. PMID 9653160.
Scheuring S, Bodor O, Röhricht RA et al. (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.
Bishop N, Woodman P (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.
Zhang QH, Ye M, Wu XY et al. (2001). "Cloning and Functional Analysis of cDNAs with Open Reading Frames for 300 Previously Undefined Genes Expressed in CD34+ Hematopoietic Stem/Progenitor Cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
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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.
Beyer A, Scheuring S, Müller S et al. (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.
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.
Fujita H, Umezuki Y, Imamura K et al. (2005). "Mammalian class E Vps proteins, SBP1 and mVps2/CHMP2A, interact with and regulate the function of an AAA-ATPase SKD1/Vps4B". J. Cell. Sci. 117 (Pt 14): 2997–3009. doi:10.1242/jcs.01170. PMID 15173323.
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.
Katoh K, Suzuki H, Terasawa Y et al. (2006). "The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B". Biochem. J. 391 (Pt 3): 677–85. doi:10.1042/BJ20050398. PMC 1276969. PMID 16004603.
Takasu H, Jee JG, Ohno A et al. (2005). "Structural characterization of the MIT domain from human Vps4b". Biochem. Biophys. Res. Commun. 334 (2): 460–5. doi:10.1016/j.bbrc.2005.06.110. PMID 16018968.
Scott A, Chung HY, Gonciarz-Swiatek M et al. (2005). "Structural and mechanistic studies of VPS4 proteins". EMBO J. 24 (20): 3658–69. doi:10.1038/sj.emboj.7600818. PMC 1276703. PMID 16193069.
Kimura K, Wakamatsu A, Suzuki Y et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Welsch S, Habermann A, Jäger S et al. (2007). "Ultrastructural analysis of ESCRT proteins suggests a role for endosome-associated tubular-vesicular membranes in ESCRT function". Traffic 7 (11): 1551–66. doi:10.1111/j.1600-0854.2006.00489.x. PMID 17014699.
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.
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.

PDB gallery

1wr0: Structural characterization of the MIT domain from human Vps4b

1xwi: Crystal Structure of VPS4B

2cpt: Solution structure of MIT domain from human SKD1

VPS4B

References

Further reading