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    CHMP3 charged multivesicular body protein 3 [ Homo sapiens (human) ]

    Gene ID: 51652, updated on 5-Mar-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    CHMP3 promotes the progression of hepatocellular carcinoma by inhibiting caspase-1-dependent pyroptosis.

    CHMP3 promotes the progression of hepatocellular carcinoma by inhibiting caspase‑1‑dependent pyroptosis.
    Zheng Y, Yang S, Dai W, Wang J, Bi S, Zhang X, Zheng Z, Sun Y, Wu S, Kong J., Free PMC Article

    12/5/2023
    A homozygous variant in CHMP3 is associated with complex hereditary spastic paraplegia.

    A homozygous variant in CHMP3 is associated with complex hereditary spastic paraplegia.
    Cohen-Barak E, Danial-Farran N, Chervinsky E, Alimi-Kasem O, Zagairy F, Livneh I, Mawassi B, Hreish M, Khayat M, Lossos A, Meiner V, Ehilevitch N, Weiss K, Shalev S.

    02/27/2023
    RetroCHMP3 blocks budding of enveloped viruses without blocking cytokinesis.

    RetroCHMP3 blocks budding of enveloped viruses without blocking cytokinesis.
    Rheinemann L, Downhour DM, Bredbenner K, Mercenne G, Davenport KA, Schmitt PT, Necessary CR, McCullough J, Schmitt AP, Simon SM, Sundquist WI, Elde NC., Free PMC Article

    01/8/2022
    miR-122-5p promotes aggression and epithelial-mesenchymal transition in triple-negative breast cancer by suppressing charged multivesicular body protein 3 through mitogen-activated protein kinase signaling.

    miR-122-5p promotes aggression and epithelial-mesenchymal transition in triple-negative breast cancer by suppressing charged multivesicular body protein 3 through mitogen-activated protein kinase signaling.
    Wang Z, Wang X.

    12/19/2020
    Protein kinase CK2 alpha 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.

    CK2 involvement in ESCRT-III complex phosphorylation.
    Salvi M, Raiborg C, Hanson PI, Campsteijn C, Stenmark H, Pinna LA.

    04/26/2014
    tight coupling of ESCRT-III CHMP3 and AMSH functions and provide insight into the regulation of ESCRT-III

    Structural basis for ESCRT-III CHMP3 recruitment of AMSH.
    Solomons J, Sabin C, Poudevigne E, Usami Y, Hulsik DL, Macheboeuf P, Hartlieb B, Göttlinger H, Weissenhorn W., Free PMC Article

    12/3/2011
    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.

    Structural basis for ESCRT-III protein autoinhibition.
    Bajorek M, Schubert HL, McCullough J, Langelier C, Eckert DM, Stubblefield WM, Uter NT, Myszka DG, Hill CP, Sundquist WI., Free PMC Article

    01/21/2010
    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

    Helical structures of ESCRT-III are disassembled by VPS4.
    Lata S, Schoehn G, Jain A, Pires R, Piehler J, Gottlinger HG, Weissenhorn W., Free PMC Article

    01/21/2010
    expression of dominant negative forms of Vps4 and Vps24, two components of the MVB pathway, rresult in an impairment in infectious herpes simplex virus assembly/egress

    Intracellular trafficking and maturation of herpes simplex virus type 1 gB and virus egress require functional biogenesis of multivesicular bodies.
    Calistri A, Sette P, Salata C, Cancellotti E, Forghieri C, Comin A, Göttlinger H, Campadelli-Fiume G, Palù G, Parolin C., Free PMC Article

    01/21/2010
    UBPY MIT domain and another ubiquitin isopeptidase, AMSH, reveals common interactions with CHMP1A and CHMP1B but a distinct selectivity of AMSH for CHMP3/VPS24, a core subunit of the ESCRT-III complex, and UBPY for CHMP7.

    The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation.
    Row PE, Liu H, Hayes S, Welchman R, Charalabous P, Hofmann K, Clague MJ, Sanderson CM, Urbé S.

    01/21/2010
    data suggest that mac25/IGFBP-rP1 and 25.1 (NEDF) may play a functional role in the NE differentiation of NSCLC cell lines and may provide a novel therapeutic target for treating lung cancers, in particular NSCLC with NE differentiation

    Neuroendocrine-like differentiation of non-small cell lung carcinoma cells: regulation by cAMP and the interaction of mac25/IGFBP-rP1 and 25.1.
    Walker GE, Antoniono RJ, Ross HJ, Paisley TE, Oh Y.

    01/21/2010
    ESCRT subunit is important for degradation of the epidermal growth factor receptor (EGFR) and for transport of the receptor from endosomes to lysosomes.

    The ESCRT-III subunit hVps24 is required for degradation but not silencing of the epidermal growth factor receptor.
    Bache KG, Stuffers S, Malerød L, Slagsvold T, Raiborg C, Lechardeur D, Wälchli S, Lukacs GL, Brech A, Stenmark H., Free PMC Article

    01/21/2010
    Data demonstrate that the VPS24 gene gives rise to two functionally distinct proteins, one of which is involved in the ESCRT pathway and another novel protein that serves an anti-apoptotic role.

    Characterization of a novel alternatively spliced human transcript encoding an N-terminally truncated Vps24 protein that suppresses the effects of Bax in an ESCRT independent manner in yeast.
    Khoury CM, Yang Z, Ismail S, Greenwood MT.

    01/21/2010
    CHMP proteins are regulated through an autoinhibitory switch mechanism that allows tight control of endosomal sorting complex ESCRT-III assembly

    Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding.
    Zamborlini A, Usami Y, Radoshitzky SR, Popova E, Palu G, Göttlinger H., Free PMC Article

    01/21/2010
    A dominant-negative version of CHMP3, which specifically prevents targeting of AMSH (STAMBP) to endosomes, inhibits degradation but not internalization of epidermal growth factor receptor.

    Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation.
    Ma YM, Boucrot E, Villén J, Affar EB, Gygi SP, Göttlinger HG, Kirchhausen T.

    01/21/2010
    In rodents, this protein selectively binds phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4-bisphosphate and may participate in endosomal trafficking.

    Identification of mammalian Vps24p as an effector of phosphatidylinositol 3,5-bisphosphate-dependent endosome compartmentalization.
    Whitley P, Reaves BJ, Hashimoto M, Riley AM, Potter BV, Holman GD.

    10/8/2004
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