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Charged multivesicular body protein 3

Vps24, CHMP3, Vps24p, hVps24, neuroendocrine differentiation factor
This gene encodes a protein that sorts 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. Read-through transcription also exists between this gene and the upstream ring finger protein 103 (RNF103) gene. [provided by RefSeq, Nov 2010] (from NCBI)
Top mentioned proteins: Vps4, Snf7, CAN, AMSH, Ubiquitin
Papers using Vps24 antibodies
One-step isolation of plasma membrane proteins using magnetic beads with immobilized concanavalin A.
Caplan Steve H., In PLoS ONE, 2007
... Rabbit polyclonal antibodies to Tsg101, ab30871, and Vps24, ab76333, were obtained from Abcam.
Papers on Vps24
Cell layer-specific distribution of transiently expressed barley ESCRT-III component HvVPS60 in developing barley endosperm.
Ibl et al., Vienna, Austria. In Protoplasma, Jan 2016
We used fluorescently tagged core ESCRT-III members HvSNF7a/CHMP4 and HvVPS24/CHMP3 and the associated ESCRT-III component HvVPS60a/CHMP5 for transient localization studies in barley endosperm.
Subviral hepatitis B virus filaments are released like infectious viral particles via multivesicular bodies.
Hildt et al., Langen, Germany. In J Virol, Jan 2016
Inhibition of MVB biogenesis by the small molecule inhibitior U18666A or inhibition of ESCRT-functionality by coexpression of transdominant negative mutants (Vps4A, Vps4B, CHMP3) abolishs the release of filaments while secretion of spheres is not affected.
Genome-wide linkage and positional association analyses identify associations of novel AFF3 and NTM genes with triglycerides: the GenSalt study.
Kelly et al., New Orleans, United States. In J Genet Genomics, Apr 2015
Follow-up analyses of these two regions revealed gene-based associations of charged multivesicular body protein 3 (CHMP3), ring finger protein 103 (RNF103), AF4/FMR2 family, member 3 (AFF3), and neurotrimin (NTM) with triglycerides (P = 4 × 10(-4), 1.00 × 10(-5), 2.00 × 10(-5), and 1.00 × 10(-7), respectively).
The ESCRT-III-interacting deubiquitinating enzyme AMSH3 is essential for degradation of ubiquitinated membrane proteins in Arabidopsis thaliana.
Isono et al., Freising, Germany. In Plant Cell Physiol, 2014
Arabidopsis AMSH3 (ASSOCIATED MOLECULE WITH THE SH3 DOMAIN OF STAM 3) is a deubiquitinating enzyme that interacts with at least two subunits of the ESCRT-III machinery, VPS2.1 and VPS24.1.
CK2 involvement in ESCRT-III complex phosphorylation.
Pinna et al., Padova, Italy. In Arch Biochem Biophys, 2014
Here we show that protein kinase CK2α is involved in the phosphorylation of the ESCRT-III subunits CHMP3 and CHMP2B, as well as of VPS4B/SKD1, an ATPase that mediates ESCRT-III disassembly.
Adenoviral expression of TDP-43 and FUS genes and shRNAs for protein degradation pathways in rodent motoneurons in vitro and in vivo.
Tsukamoto et al., Tokyo, Japan. In Neuropathology, 2014
In the present study, we produced recombinant adenovirus vectors encoding wild type and mutant TDP-43 and FUS, and those encoding short hairpin RNAs (shRNAs) for proteasome (PSMC1), autophagy (ATG5), and endosome (VPS24) systems to investigate whether the coupled gene transductions in motoneurons by these adenoviruses elicit ALS pathology.
A complex network of interactions between mitotic kinases, phosphatases and ESCRT proteins regulates septation and membrane trafficking in S. pombe.
McInerny et al., Glasgow, United Kingdom. In Plos One, 2013
Multiple observations indicate functional interplay between polo and ESCRT components: firstly, two-hybrid in vivo interactions are reported between Plo1p and Sst4p, Vps28p, Vps25p, Vps20p and Vps32p; secondly, co-immunoprecipitation of human homologues of Vps20p, Vps32p, Vps24p and Vps2p by human Plk1; and thirdly, in vitro phosphorylation of budding yeast Vps32p and Vps20p by polo kinase.
ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding.
Weissenhorn et al., Grenoble, France. In Cell Microbiol, 2013
We have used electron cryomicroscopy to determine the molecular organization of pleiomorphic ESCRT-III CHMP2A-CHMP3 polymers.
In vitro reconstitution of the ordered assembly of the endosomal sorting complex required for transport at membrane-bound HIV-1 Gag clusters.
Hurley et al., Bethesda, United States. In Proc Natl Acad Sci U S A, 2012
However, the full pathway of ESCRT recruitment to HIV-1 budding sites, which culminates with the assembly of the late-acting CHMP4, CHMP3, CHMP2, and CHMP1 subunits, is less completely understood.
Echovirus 1 infection depends on biogenesis of novel multivesicular bodies.
Marjomäki et al., Jyväskylä, Finland. In Cell Microbiol, 2011
Furthermore, α2-MVBs were positive for some members of ESCRTs such as Hrs, VPS37A and VPS24 and the siRNA treatment of TSG101, VPS37A and VPS24 inhibited EV1 infection.
GLUT4 traffic through an ESCRT-III-dependent sorting compartment in adipocytes.
Holman et al., Bath, United Kingdom. In Plos One, 2011
Introduction of the dominant negative inhibitory constructs of the ESCRT-III components CHMP3 (CHMP3(1-179)) and Vps4 (GFP-Vps4(E235Q)) into rat adipocytes leads to the accumulation of GLUT4 in large, coalesced and extended vesicles structures that co-localise with the inhibitory constructs over large parts of the extended structure.
Charged multivesicular body protein 2B (CHMP2B) of the endosomal sorting complex required for transport-III (ESCRT-III) polymerizes into helical structures deforming the plasma membrane.
Sadoul et al., Grenoble, France. In J Biol Chem, 2011
In vitro, CHMP2 and CHMP3 recombinant proteins polymerize into tubular helical structures, which were hypothesized to drive vesicle fission.
Structural basis for ESCRT-III CHMP3 recruitment of AMSH.
Weissenhorn et al., Grenoble, France. In Structure, 2011
tight coupling of ESCRT-III CHMP3 and AMSH functions and provide insight into the regulation of ESCRT-III
ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formation.
Emr et al., Innsbruck, Austria. In Embo J, 2010
ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formation.
Structural basis for ESCRT-III protein autoinhibition.
Sundquist et al., Salt Lake City, United States. In Nat Struct Mol Biol, 2009
Data show that the N-terminal core domains of increased sodium tolerance-1 (IST1) and charged multivesicular body protein-3 (CHMP3) form equivalent four-helix bundles, revealing that IST1 is a previously unrecognized ESCRT-III family member.
Structure and function of ESCRT-III.
Weissenhorn et al., Grenoble, France. In Biochem Soc Trans, 2009
At least CHMP (charged multivesicular body protein) 2A and CHMP3 assemble into helical tubular structures that provide a platform for membrane interaction and VPS (vacuolar protein sorting) 4-catalysed effects leading to disassembly of ESCRT-III CHMP2A-CHMP3 polymers in vitro.
Structure and disassembly of filaments formed by the ESCRT-III subunit Vps24.
Williams et al., Cambridge, United Kingdom. In Structure, 2008
Structure and disassembly of filaments formed by the ESCRT-III subunit Vps24.
Helical structures of ESCRT-III are disassembled by VPS4.
Weissenhorn et al., Grenoble, France. In Science, 2008
study found the ESCRT-III proteins CHMP2A & CHMP3 could assemble in vitro into helical tubular structures that expose their membrane interaction sites on the outside of the tubule; VPS4 could bind on the inside of the tubule & disassemble the tubes
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