Gene Symbol: Dnajc3
Description: DnaJ heat shock protein family (Hsp40) member C3
Alias: dnaJ homolog subfamily C member 3, DnaJ (Hsp40) homolog, subfamily C, member 3, interferon-induced, double-stranded RNA-activated protein kinase inhibitor, protein kinase inhibitor of 58 kDa, protein kinase inhibitor p58
Species: rat
Products:     Dnajc3

Top Publications

  1. Yan W, Frank C, Korth M, Sopher B, Novoa I, Ron D, et al. Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK. Proc Natl Acad Sci U S A. 2002;99:15920-5 pubmed
    ..Our studies suggest that P58(IPK) induction during the ER-stress response represses PERK activity and plays a functional role in the expression of downstream markers of PERK activity in the later phase of the ER-stress response. ..
  2. Yang H, Liu R, Cui Z, Chen Z, Yan S, Pei H, et al. Functional characterization of 58-kilodalton inhibitor of protein kinase in protecting against diabetic retinopathy via the endoplasmic reticulum stress pathway. Mol Vis. 2011;17:78-84 pubmed
    ..These results revealed the protecting role of P58(IPK) against ER stress-mediated DR in diabetic rats, suggesting that P58(IPK) may act as a DR-resistant gene during diabetes. ..
  3. Huber A, Lebeau J, Guillaumot P, Petrilli V, Malek M, Chilloux J, et al. p58(IPK)-mediated attenuation of the proapoptotic PERK-CHOP pathway allows malignant progression upon low glucose. Mol Cell. 2013;49:1049-59 pubmed publisher
    ..Altogether, these results show that ER stress activation and p58(IPK) expression control the fate of malignant cells facing glucose shortage. ..
  4. Gao D, Bambang I, Putti T, Lee Y, Richardson D, Zhang D. ERp29 induces breast cancer cell growth arrest and survival through modulation of activation of p38 and upregulation of ER stress protein p58IPK. Lab Invest. 2012;92:200-13 pubmed publisher
    ..Hence, the interplay between p38 phosphorylation and p58(IPK) upregulation has key roles in modulating ERp29-induced cell-growth arrest and survival. ..
  5. Jansen G, Maattanen P, Denisov A, Scarffe L, Schade B, Balghi H, et al. An interaction map of endoplasmic reticulum chaperones and foldases. Mol Cell Proteomics. 2012;11:710-23 pubmed publisher
  6. Roobol A, Roobol J, Bastide A, Knight J, Willis A, Smales C. p58IPK is an inhibitor of the eIF2α kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacity. Biochem J. 2015;465:213-25 pubmed publisher
  7. Korth M, Lyons C, Wambach M, Katze M. Cloning, expression, and cellular localization of the oncogenic 58-kDa inhibitor of the RNA-activated human and mouse protein kinase. Gene. 1996;170:181-8 pubmed
  8. Oyadomari S, Yun C, Fisher E, Kreglinger N, Kreibich G, Oyadomari M, et al. Cotranslocational degradation protects the stressed endoplasmic reticulum from protein overload. Cell. 2006;126:727-39 pubmed
    ..Here, we report that P58(IPK)/DNAJC3, a UPR-responsive gene previously implicated in translational control, encodes a cytosolic cochaperone that ..
  9. Petrova K, Oyadomari S, Hendershot L, Ron D. Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3. EMBO J. 2008;27:2862-72 pubmed publisher
    P58/DNAJc3 defends cells against endoplasmic reticulum (ER) stress. Most P58 molecules are translocated into the ER lumen, and here we report selective and stable binding to misfolded proteins by P58's TPR-containing N-terminal domain...