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    PSMD4 proteasome 26S subunit ubiquitin receptor, non-ATPase 4 [ Homo sapiens (human) ]

    Gene ID: 5710, updated on 4-Jan-2025

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    PSMD4 drives progression of hepatocellular carcinoma via Akt/COX2 pathway and p53 inhibition.

    PSMD4 drives progression of hepatocellular carcinoma via Akt/COX2 pathway and p53 inhibition.
    Zhang J, Fang S, Rong F, Jia M, Wang Y, Cui H, Hao P.

    08/25/2023
    Upregulation of Rpn10 promotes tumor progression via activation of the NF-kappaB pathway in clear cell renal cell carcinoma.

    Upregulation of Rpn10 promotes tumor progression via activation of the NF-κB pathway in clear cell renal cell carcinoma.
    Huang T, Tian W, Zhou Q, Li J, Jiang Z, Chen J, Ge C, Tian H.

    08/7/2021
    The role of endogenous Antisecretory Factor (AF) in the treatment of Meniere's Disease: A two-year follow-up study. Preliminary results.

    The role of endogenous Antisecretory Factor (AF) in the treatment of Ménière's Disease: A two-year follow-up study. Preliminary results.
    Viola P, Pisani D, Scarpa A, Cassandro C, Laria C, Aragona T, Ciriolo M, Spadera L, Ralli M, Cavaliere M, Iengo M, Chiarella G.

    12/19/2020
    E6AP/UBE3A is distinguished from other E3 ligases by having a 12 nM binding site at the proteasome contributed by substrate receptor hRpn10/PSMD4/S5a.

    Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10.
    Buel GR, Chen X, Chari R, O'Neill MJ, Ebelle DL, Jenkins C, Sridharan V, Tarasov SG, Tarasova NI, Andresson T, Walters KJ., Free PMC Article

    07/11/2020
    Data shows upregulation of PSMD4 promoted the progression of esophageal cancer mainly by reducing ERS-induced cell apoptosis.

    PSMD4 regulates the malignancy of esophageal cancer cells by suppressing endoplasmic reticulum stress.
    Ma AG, Yu LM, Zhao H, Qin CW, Tian XY, Wang Q.

    05/2/2020
    UBQLN2 UBL is fine-tuned for the hRpn10 UIM-1 site.

    Structure of hRpn10 Bound to UBQLN2 UBL Illustrates Basis for Complementarity between Shuttle Factors and Substrates at the Proteasome.
    Chen X, Ebelle DL, Wright BJ, Sridharan V, Hooper E, Walters KJ., Free PMC Article

    03/7/2020
    Rpn10 directly promoted PTEN degradation.

    Rpn10 promotes tumor progression by regulating hypoxia-inducible factor 1 alpha through the PTEN/Akt signaling pathway in hepatocellular carcinoma.
    Jiang Z, Zhou Q, Ge C, Yang J, Li H, Chen T, Xie H, Cui Y, Shao M, Li J, Tian H.

    12/14/2019
    Two Angelman syndrome point mutations of UBE3A that affect the AZUL domain show an impaired ability to bind PSMD4.

    Angelman syndrome-associated point mutations in the Zn(2+)-binding N-terminal (AZUL) domain of UBE3A ubiquitin ligase inhibit binding to the proteasome.
    Kühnle S, Martínez-Noël G, Leclere F, Hayes SD, Harper JW, Howley PM., Free PMC Article

    06/29/2019
    Findings indicated PSMD4 as a subunit of 26S proteasome exerts as an oncogene during tumor development of hepatocellular carcinoma.

    Inhibition of PSMD4 blocks the tumorigenesis of hepatocellular carcinoma.
    Cai MJ, Cui Y, Fang M, Wang Q, Zhang AJ, Kuai JH, Pang F, Cui XD.

    05/18/2019
    Preterm delivery is associated with low levels of anti-secretory factor in placenta. Inflammation, a potential trigger of preterm birth, is more pronounced in the preterm placenta and inversely related to the placental level of anti-secretory factor.

    Low levels of anti-secretory factor in placenta are associated with preterm birth and inflammation.
    Gustafsson AM, Fransson E, Dubicke A, Hjelmstedt AK, Ekman-Ordeberg G, Silfverdal SA, Lange S, Jennische E, Bohlin K.

    11/3/2018
    We therefore suggest that PSMD4 or b-catenin might be potential targets for suppressing tumor aggressiveness, and consequently, improving outcomes in patients whose tumors express cNrf2.

    Cytoplasmic localization of Nrf2 promotes colorectal cancer with more aggressive tumors via upregulation of PSMD4.
    Lin PL, Chang JT, Wu DW, Huang CC, Lee H.

    12/23/2017
    Binding (especially high-affinity binding) of non-ubiquitinated proteins to the Rpn10 proteasome subunit can both regulate the functioning of this proteasomal ubiquitin receptor (by competing with ubiquitinated substrates) and promote activation of other pathways for proteolytic degradation of proteins destined to the proteasome.

    Quantitative Affinity Interaction of Ubiquitinated and Non-ubiquitinated Proteins with Proteasome Subunit Rpn10.
    Buneeva OA, Gnedenko OV, Kopylov AT, Medvedeva MV, Zgoda VG, Ivanov AS, Medvedev AE.

    11/4/2017
    The platelet 26S proteasome exhibits different basal activities of its catalytic subunits and chymotrypsin-like activity is most prominently enhanced by calcium dependent signaling. Collagen stimulation enhances 26S proteasome chymotrypsin-like activity in platelets.

    The proteasome regulates collagen-induced platelet aggregation via nuclear-factor-kappa-B (NFĸB) activation.
    Grundler K, Rotter R, Tilley S, Pircher J, Czermak T, Yakac M, Gaitzsch E, Massberg S, Krötz F, Sohn HY, Pohl U, Mannell H, Kraemer BF.

    04/22/2017
    regulation of NY-ESO-1 processing by the ubiquitin receptors Rpn10 and Rpn13 as a well as by the standard and immunoproteasome is governed by non-canonical ubiquitination on non-lysine sites.

    Major Histocompatibility Complex (MHC) Class I Processing of the NY-ESO-1 Antigen Is Regulated by Rpn10 and Rpn13 Proteins and Immunoproteasomes following Non-lysine Ubiquitination.
    Golnik R, Lehmann A, Kloetzel PM, Ebstein F., Free PMC Article

    10/8/2016
    Not only AF1, but an entire proteasome complex, seems to be present in blood.

    Interaction of Proteasomes and Complement C3, Assay of Antisecretory Factor in Blood.
    Lönnroth I, Oshalim M, Lange S, Johansson E.

    10/8/2016
    binds to death receptor-6, and induces monocyte cell line differentiation via NF-kB pathway

    S5a binds to death receptor-6 to induce THP-1 monocytes to differentiate through the activation of the NF-κB pathway.
    Wang Z, Fan C, Zhou HF, Lu JS, Sun MJ, Song JW, Le Y, Jiang HD, Wang LH, Jiao BH.

    10/24/2015
    The VWA domain regulation of ubiquitin and Ubl binding to S5a is restricted to the 26S proteasome.

    VWA domain of S5a restricts the ability to bind ubiquitin and Ubl to the 26S proteasome.
    Piterman R, Braunstein I, Isakov E, Ziv T, Navon A, Cohen S, Stanhill A., Free PMC Article

    08/22/2015
    The degradation of TP53 and MDM2 by the proteasome can be selectively dependent on S5a in human cells.

    The degradation of p53 and its major E3 ligase Mdm2 is differentially dependent on the proteasomal ubiquitin receptor S5a.
    Sparks A, Dayal S, Das J, Robertson P, Menendez S, Saville MK., Free PMC Article

    11/22/2014
    To examine angiocidin expression in SMMC-7221 and HepG2 cells and the role of angiocidin in liver cancer cell growth. Angiocidin is highly expressed in liver cancer cells, and it may play a key role in tumor growth of liver cancers.

    Reduction of angiocidin contributes to decreased HepG2 cell proliferation.
    Guan XG, Guan XQ, Feng K, Jian R, Tian D, Tian D, Tong HB, Sun X., Free PMC Article

    09/13/2014
    Authors demonstrate that human cytomegalovirus UL76 induces a novel nuclear aggresome, likely by subverting S5a of the ubiquitin-proteasome system.

    Human cytomegalovirus UL76 elicits novel aggresome formation via interaction with S5a of the ubiquitin proteasome system.
    Lin SR, Jiang MJ, Wang HH, Hu CH, Hsu MS, Hsi E, Duh CY, Wang SK., Free PMC Article

    11/30/2013
    One consequence of the interaction between E6/E6AP and S5a is enhanced ubiquitination of this proteasome subunit.

    Interaction of HPV E6 oncoproteins with specific proteasomal subunits.
    Tomaić V, Ganti K, Pim D, Bauer C, Blattner C, Banks L.

    11/23/2013
    These studies suggest that diminished 26S activity in failing human hearts may be related ti impaired docking of the 19S to the 20S as a result of decreased Rpt subunit ATPase activity and alpha7 subunit phosphorylation.

    Impaired assembly and post-translational regulation of 26S proteasome in human end-stage heart failure.
    Day SM, Divald A, Wang P, Davis F, Bartolone S, Jones R, Powell SR., Free PMC Article

    07/27/2013
    identified the VWA domain of hRpn10 as a receptor for ubiquitin-like proteins within the 26S proteasome and elucidated how FAT10 mediates efficient proteolysis by the proteasome

    FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis.
    Rani N, Aichem A, Schmidtke G, Kreft SG, Groettrup M.

    08/4/2012
    Both higher PSMD4 expression levels and higher 1q21 copy numbers affected clinical outcome adversely.

    Pharmacogenomics of bortezomib test-dosing identifies hyperexpression of proteasome genes, especially PSMD4, as novel high-risk feature in myeloma treated with Total Therapy 3.
    Shaughnessy JD Jr, Qu P, Usmani S, Heuck CJ, Zhang Q, Zhou Y, Tian E, Hanamura I, van Rhee F, Anaissie E, Epstein J, Nair B, Stephens O, Williams R, Waheed S, Alsayed Y, Crowley J, Barlogie B., Free PMC Article

    12/3/2011
    results suggest that there is different substrate specificity between S5a and hRpn13 at the level of delivery and S5a may be the major docking site for ERAD substrates.

    Functional differences between two major ubiquitin receptors in the proteasome; S5a and hRpn13.
    Elangovan M, Oh C, Sukumaran L, Wójcik C, Yoo YJ.

    07/12/2010
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