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    Dnajc3 DnaJ heat shock protein family (Hsp40) member C3 [ Mus musculus (house mouse) ]

    Gene ID: 100037258, updated on 8-Mar-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Congenital Hyperinsulinism in Humans and Insulin Secretory Dysfunction in Mice Caused by Biallelic DNAJC3 Variants.

    Congenital Hyperinsulinism in Humans and Insulin Secretory Dysfunction in Mice Caused by Biallelic DNAJC3 Variants.
    Welters A, Nortmann O, Wörmeyer L, Freiberg C, Eberhard D, Bachmann N, Bergmann C, Mayatepek E, Meissner T, Kummer S., Free PMC Article

    02/2/2024
    Progranulin inhibits fibrosis by interacting with and up-regulating DNAJC3 during mouse skin wound healing.

    Progranulin inhibits fibrosis by interacting with and up-regulating DNAJC3 during mouse skin wound healing.
    Li S, Liu J, Guo J, Xu Y, Zhou Z, Li Z, Cai H.

    09/6/2023
    Neuronal p58[IPK] Protects Retinal Ganglion Cells Independently of Macrophage/Microglia Activation in Ocular Hypertension.

    Neuronal p58(IPK) Protects Retinal Ganglion Cells Independently of Macrophage/Microglia Activation in Ocular Hypertension.
    McLaughlin T, Wang J, Jia L, Wu F, Wang Y, Wang JJ, Mu X, Zhang SX., Free PMC Article

    06/30/2023
    Chaperone protein p58(IPK) is expressed predominantly in retinal ganglion cells (RGC), inner retinal neurons, and the photoreceptor inner segments.

    Identification of p58IPK as a novel neuroprotective factor for retinal neurons.
    Boriushkin E, Wang JJ, Li J, Jing G, Seigel GM, Zhang SX., Free PMC Article

    04/11/2015
    p58IPK is a general inhibitor of the eIF2alpha kinases in that it also interacts with GCN2. Thus forced overexpression of cytoplasmic p58 delays eIF2alpha phosphorylation, suppresses GCN2 phosphorylation and prolongs protein synthesis

    p58IPK is an inhibitor of the eIF2α kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacity.
    Roobol A, Roobol J, Bastide A, Knight JR, Willis AE, Smales CM.

    03/21/2015
    combined deletion of ATF6alpha and the ER cochaperone p58(IPK) resulted in synthetic embryonic lethality.

    Synthetic embryonic lethality upon deletion of the ER cochaperone p58(IPK) and the ER stress sensor ATF6α.
    Gomez JA, Tyra HM, DeZwaan-McCabe D, Olivier AK, Rutkowski DT., Free PMC Article

    05/10/2014
    Data present a working model for P58(IPK) to act together with Bip to prevent protein aggregations and promote protein foldings within ER.

    Structural insight into the protective role of P58(IPK) during unfolded protein response.
    Tao J, Sha B.

    04/23/2011
    Coxsackievirus B3 infection induces apoptosis through downregulation of p58IPK and activation of CHOP and SREBP1.

    Coxsackievirus B3 infection activates the unfolded protein response and induces apoptosis through downregulation of p58IPK and activation of CHOP and SREBP1.
    Zhang HM, Ye X, Su Y, Yuan J, Liu Z, Stein DA, Yang D., Free PMC Article

    09/20/2010
    mechanism by which P58(IPK) functions to promote protein folding within the endoplasmic reticulum, determined from the crystal structure of P58(IPK)

    Crystal structure of P58(IPK) TPR fragment reveals the mechanism for its molecular chaperone activity in UPR.
    Tao J, Petrova K, Ron D, Sha B., Free PMC Article

    05/31/2010
    renal injury inflicted by expression of the folding mutants was markedly enhanced by haploinsufficiency of the endoplasmic reticulum cochaperone p58(IPK).

    Progressive renal injury from transgenic expression of human carbonic anhydrase IV folding mutants is enhanced by deficiency of p58IPK.
    Datta R, Shah GN, Rubbelke TS, Waheed A, Rauchman M, Goodman AG, Katze MG, Sly WS., Free PMC Article

    05/10/2010
    Results show that P58(IPK) is activated during virus infection to inhibit virus-induced apoptosis and inflammation to prolong host survival, even while prolonging viral replication.

    P58(IPK): a novel "CIHD" member of the host innate defense response against pathogenic virus infection.
    Goodman AG, Fornek JL, Medigeshi GR, Perrone LA, Peng X, Dyer MD, Proll SC, Knoblaugh SE, Carter VS, Korth MJ, Nelson JA, Tumpey TM, Katze MG., Free PMC Article

    01/21/2010
    Selective and stable binding to misfolded proteins by P58's TPR-containing N-terminal domain, is reported.

    Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3.
    Petrova K, Oyadomari S, Hendershot LM, Ron D., Free PMC Article

    01/21/2010
    investigated the mechanism by which P58(IPK) functions to promote protein folding within the ER, cy crystallizing a P58(IPK) TPR fragment without the C-terminal J-domain

    Preliminary X-ray crystallographic studies of mouse UPR responsive protein P58(IPK) TPR fragment.
    Tao J, Wu Y, Ron D, Sha B., Free PMC Article

    01/21/2010
    These results identify a previously unanticipated location for p58(IPK) in the ER lumen where its putative function as a cochaperone explains the stress-sensitivity phenotype of knockout cells and mice.

    The role of p58IPK in protecting the stressed endoplasmic reticulum.
    Rutkowski DT, Kang SW, Goodman AG, Garrison JL, Taunton J, Katze MG, Kaufman RJ, Hegde RS., Free PMC Article

    01/21/2010
    absence of P58(IPK) led to an increase in eIF2alpha phosphorylation and decreased influenza virus mRNA translation

    The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-mediated mechanism.
    Goodman AG, Smith JA, Balachandran S, Perwitasari O, Proll SC, Thomas MJ, Korth MJ, Barber GN, Schiff LA, Katze MG., Free PMC Article

    01/21/2010
    The stress of unfolded proteins in the ER activates P58(IPK) transcription through an ER stress-response element in its promoter. P58(IPK) interacts with & inhibits PERK, which protects cells during the ER-stress response by reducing protein synthesis.

    Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK.
    Yan W, Frank CL, Korth MJ, Sopher BL, Novoa I, Ron D, Katze MG., Free PMC Article

    01/21/2010
    Insulin deficiency associated with the absence of P58(IPK) mimics beta-cell failure associated with type 1 and late-stage type 2 diabetes.

    Pancreatic beta-cell failure and diabetes in mice with a deletion mutation of the endoplasmic reticulum molecular chaperone gene P58IPK.
    Ladiges WC, Knoblaugh SE, Morton JF, Korth MJ, Sopher BL, Baskin CR, MacAuley A, Goodman AG, LeBoeuf RC, Katze MG.

    01/21/2010
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