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    PSMD2 proteasome 26S subunit ubiquitin receptor, non-ATPase 2 [ Homo sapiens (human) ]

    Gene ID: 5708, updated on 6-Oct-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    DNAJA4 suppresses epithelial-mesenchymal transition and metastasis in nasopharyngeal carcinoma via PSMD2-mediated MYH9 degradation.

    DNAJA4 suppresses epithelial-mesenchymal transition and metastasis in nasopharyngeal carcinoma via PSMD2-mediated MYH9 degradation.
    Zhang Q, Feng P, Zhu XH, Zhou SQ, Ye ML, Yang XJ, Gong S, Huang SY, Tan XR, He SW, Li YQ., Free PMC Article

    10/28/2023
    Proteasomal Degradation of TRAF2 Mediates Mitochondrial Dysfunction in Doxorubicin-Cardiomyopathy.

    Proteasomal Degradation of TRAF2 Mediates Mitochondrial Dysfunction in Doxorubicin-Cardiomyopathy.
    Dhingra R, Rabinovich-Nikitin I, Rothman S, Guberman M, Gang H, Margulets V, Jassal DS, Alagarsamy KN, Dhingra S, Valenzuela Ripoll C, Billia F, Diwan A, Javaheri A, Kirshenbaum LA., Free PMC Article

    10/8/2022
    Diverse Ras-related GTPase DIRAS2, downregulated by PSMD2 in a proteasome-mediated way, inhibits colorectal cancer proliferation by blocking NF-kappaB signaling.

    Diverse Ras-related GTPase DIRAS2, downregulated by PSMD2 in a proteasome-mediated way, inhibits colorectal cancer proliferation by blocking NF-κB signaling.
    Ying K, Wang C, Liu S, Kuang Y, Tao Q, Hu X., Free PMC Article

    04/23/2022
    TRAF2 Knockdown in Nasopharyngeal Carcinoma Induced Cell Cycle Arrest and Enhanced the Sensitivity to Radiotherapy.

    TRAF2 Knockdown in Nasopharyngeal Carcinoma Induced Cell Cycle Arrest and Enhanced the Sensitivity to Radiotherapy.
    Zhu H, Ding W, Wu J, Ma R, Pan Z, Mao X., Free PMC Article

    03/27/2021
    The authors demonstrate that PSMD1 and PSMD2 promote the proliferation of HepG2 cells via facilitating cellular lipid droplet accumulation.

    PSMD1 and PSMD2 regulate HepG2 cell proliferation and apoptosis via modulating cellular lipid droplet metabolism.
    Tan Y, Jin Y, Wu X, Ren Z., Free PMC Article

    04/11/2020
    Asporin (ASPN) interacts with proteasome 26S subunit non-ATPase 2 (PSMD2) and promotes the proliferation of gastric cancer (GC) cells.

    Asporin promotes cell proliferation via interacting with PSMD2 in gastric cancer.
    Zhang Z, Li H, Zhao Y, Guo Q, Yu Y, Zhu S, Zhang S, Min L, Li P.

    01/4/2020
    Study found that PSMD2 was markedly upregulated in breast cancer. High PSMD2 expression was significantly correlated with poor prognosis. PSMD2 knockdown inhibited cell proliferation and arrested cell cycle at G0/G1 phase in vitro, as well as suppressed tumor growth in vivo. Mechanically, PSMD2 physically interacted with p21 and p27 and mediated their ubiquitin-proteasome degradation with the cooperation of USP14.

    PSMD2 regulates breast cancer cell proliferation and cell cycle progression by modulating p21 and p27 proteasomal degradation.
    Li Y, Huang J, Zeng B, Yang D, Sun J, Yin X, Lu M, Qiu Z, Peng W, Xiang T, Li H, Ren G.

    08/10/2019
    By recruiting the 26S proteasome and the ubiquitin-selective ATPase p97 to arsenite-induced stress granules, ZFAND1 ensures their timely clearance and prevents their aberration.

    ZFAND1 Recruits p97 and the 26S Proteasome to Promote the Clearance of Arsenite-Induced Stress Granules.
    Turakhiya A, Meyer SR, Marincola G, Böhm S, Vanselow JT, Schlosser A, Hofmann K, Buchberger A.

    03/9/2019
    the high-resolution solution structure of the UBL domain of human UBLCP1 and its interaction with Rpn1

    Solution structure and Rpn1 interaction of the UBL domain of human RNA polymerase II C-terminal domain phosphatase.
    Yun JH, Ko S, Lee CK, Cheong HK, Cheong C, Yoon JB, Lee W., Free PMC Article

    12/14/2013
    Results suggest that PSMD2 may be a good molecular target candidate.

    Proteasomal non-catalytic subunit PSMD2 as a potential therapeutic target in association with various clinicopathologic features in lung adenocarcinomas.
    Matsuyama Y, Suzuki M, Arima C, Huang QM, Tomida S, Takeuchi T, Sugiyama R, Itoh Y, Yatabe Y, Goto H, Takahashi T.

    06/18/2011
    These data suggest that p97 recruits proteasomes to polytopic ER proteins, such as Insig-1, even before they are extracted from membranes.

    Regulated endoplasmic reticulum-associated degradation of a polytopic protein: p97 recruits proteasomes to Insig-1 before extraction from membranes.
    Ikeda Y, Demartino GN, Brown MS, Lee JN, Goldstein JL, Ye J., Free PMC Article

    02/8/2010
    the 26S proteasome may provide a general predictive biomarker for radiotherapy outcome.

    Proteomic identification of putative biomarkers of radiotherapy resistance: a possible role for the 26S proteasome?
    Smith L, Qutob O, Watson MB, Beavis AW, Potts D, Welham KJ, Garimella V, Lind MJ, Drew PJ, Cawkwell L., Free PMC Article

    01/21/2010
    Data show that data provide a novel mechanism whereby CaMKII may regulate the proteasome in neurons to facilitate remodeling of synaptic connections through protein degradation.

    Regulation of the proteasome by neuronal activity and calcium/calmodulin-dependent protein kinase II.
    Djakovic SN, Schwarz LA, Barylko B, DeMartino GN, Patrick GN., Free PMC Article

    01/21/2010
    Observational study of gene-disease association. (HuGE Navigator)See all PubMed (2) articles

    Investigation of genetic susceptibility factors for human longevity - a targeted nonsynonymous SNP study.
    Flachsbart F, Franke A, Kleindorp R, Caliebe A, Blanché H, Schreiber S, Nebel A.

    Follow-up examination of linkage and association to chromosome 1q43 in multiple sclerosis.
    McCauley JL, Zuvich RL, Bradford Y, Kenealy SJ, Schnetz-Boutaud N, Gregory SG, Hauser SL, Oksenberg JR, Mortlock DP, Pericak-Vance MA, Haines JL.

    09/20/2009
    U87 glioblastoma cells transduced to express the epidermal growth factor receptor vIII (EGFRvIII) mutant do not respond toirrradiation with 26s proteasome inhibition.

    Epidermal growth factor receptor vIII expression in U87 glioblastoma cells alters their proteasome composition, function, and response to irradiation.
    Kim K, Brush JM, Watson PA, Cacalano NA, Iwamoto KS, McBride WH., Free PMC Article

    01/21/2010
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