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    Adrm1 adhesion regulating molecule 1 26S proteasome ubiquitin receptor [ Mus musculus (house mouse) ]

    Gene ID: 56436, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Here, the authors show that Shigella flexneri invasion plasmid antigen H (IpaH) 4.5, a member of the E3 ubiquitin ligase effector family, targets the proteasome regulatory particle non-ATPase 13 (RPN13) and induces its degradation via the ubiquitin-proteasome system (UPS).

    Shigella effector IpaH4.5 targets 19S regulatory particle subunit RPN13 in the 26S proteasome to dampen cytotoxic T lymphocyte activation.
    Otsubo R, Mimuro H, Ashida H, Hamazaki J, Murata S, Sasakawa C.

    05/16/2020
    ADRM1-dependent ubiquitin proteasome system (UPS) may be a general mechanism to guard cells from mutant Htt toxicity

    The Ubiquitin Receptor ADRM1 Modulates HAP40-Induced Proteasome Activity.
    Huang ZN, Her LS.

    05/11/2019
    studies suggest that HAP40-mediated reduction of ADRM1 alters the mitochondrial fission activity and results in mitochondrial fragmentation and mitochondrial dysfunction.

    Adhesion Regulating Molecule 1 Mediates HAP40 Overexpression-Induced Mitochondrial Defects.
    Huang ZN, Chung HM, Fang SC, Her LS., Free PMC Article

    09/1/2018
    Data show that either Rpn13 knock down or RA190 treatment reduced the capacity of myeloid-derived-suppressor cells (MDSCs) to suppress T cell proliferation in vitro.

    RPN13/ADRM1 inhibitor reverses immunosuppression by myeloid-derived suppressor cells.
    Soong RS, Anchoori RK, Yang B, Yang A, Tseng SH, He L, Tsai YC, Roden RB, Hung CF., Free PMC Article

    02/17/2018
    the binding of SGTA to Rpn13 enables specific polypeptides to escape proteasomal degradation and/or selectively modulates substrate degradation.

    Binding of SGTA to Rpn13 selectively modulates protein quality control.
    Leznicki P, Korac-Prlic J, Kliza K, Husnjak K, Nyathi Y, Dikic I, High S., Free PMC Article

    06/4/2016
    this study showed that Rpn13 plays a redundant role with Rpn10 in recognition and degradation of ubiquitinated proteins in mouse livers.

    Redundant Roles of Rpn10 and Rpn13 in Recognition of Ubiquitinated Proteins and Cellular Homeostasis.
    Hamazaki J, Hirayama S, Murata S., Free PMC Article

    05/7/2016
    this is the first report characterizing the physiological roles of Uch37 and Rpn13 in murine development and implicating a non-ATPase proteasomal protein, Rpn13, in the process of gametogenesis

    Regulators of the proteasome pathway, Uch37 and Rpn13, play distinct roles in mouse development.
    Al-Shami A, Jhaver KG, Vogel P, Wilkins C, Humphries J, Davis JJ, Xu N, Potter DG, Gerhardt B, Mullinax R, Shirley CR, Anderson SJ, Oravecz T., Free PMC Article

    03/12/2011
    show that Rpn13 is involved in inducible nitric oxide synthase degradation and is required for iNOS interaction with the deubiquitination protein UCH37.

    Regulation of NF-kappaB activity and inducible nitric oxide synthase by regulatory particle non-ATPase subunit 13 (Rpn13).
    Mazumdar T, Gorgun FM, Sha Y, Tyryshkin A, Zeng S, Hartmann-Petersen R, Jørgensen JP, Hendil KB, Eissa NT., Free PMC Article

    09/13/2010
    crystallography and NMR data to describe the ubiquitin-binding mechanism of Rpn13

    Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction.
    Schreiner P, Chen X, Husnjak K, Randles L, Zhang N, Elsasser S, Finley D, Dikic I, Walters KJ, Groll M., Free PMC Article

    01/21/2010
    identification of a new ubiquitin receptor, Rpn13/ARM1, a known component of the proteasome

    Proteasome subunit Rpn13 is a novel ubiquitin receptor.
    Husnjak K, Elsasser S, Zhang N, Chen X, Randles L, Shi Y, Hofmann K, Walters KJ, Finley D, Dikic I., Free PMC Article

    01/21/2010
    ARM-1 is a cytosolic protein associated with the plasma membrane. However, no cell surface expression of the protein was observed. These results suggest an indirect role of ARM-1 in adhesion rather than a direct role as an adhesion molecule itself.

    Adhesion properties of adhesion-regulating molecule 1 protein on endothelial cells.
    Lamerant N, Kieda C.

    01/21/2010
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