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DNAJC3 p.H238N is likely to be a variant causing diabetes.
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
Loss-of-function DNAJC3 mutations lead to a monogenic, recessive form of diabetes mellitus in humans.
p58(IPK) suppresses coxsackievirus B3-induced apoptosis through selective activation of PI3K/Akt pathway that requires activation of ATF6a and subsequently upregulates mitofusin 2.
interplay between p38 phosphorylation and p58(IPK) upregulation has key roles in modulating ERp29-induced cell-growth arrest and survival
the crystal structure of human P58(IPK)
Coxsackievirus B3 infection induces apoptosis through downregulation of p58IPK and activation of CHOP and SREBP1.
Spleen cells from transgenic mice overexpressing (Hu)PKR were studied and compared to those from wild-type mice after drug treatment. Dact-treated spleen cells were resistant to apoptosis; ConA-treated cells had decreased cell division.
P58(IPK) is an important component of a negative feedback loop used by the cell to inhibit eIF2alpha signaling, and thus attenuate the unfolded protein response.
The study demonstrates that P58(IPK) inhibits endoplasmic reticulum (ER) stress and plays an important role in maintaining balance and stability of the ER in human retinal capillary endothelial cells.
The sequence and structure of pP58IPK was highly similar to the counterpart of human.
Cloning, prokaryotic expression of novel swine gene P58IPK and its polyclonal antibody preparation
Chaperone protein p58(IPK) is expressed predominantly in retinal ganglion cells (RGC), inner retinal neurons, and the photoreceptor inner segments.
combined deletion of ATF6alpha and the ER cochaperone p58(IPK) resulted in synthetic embryonic lethality.
Data present a working model for P58(IPK) to act together with Bip to prevent protein aggregations and promote protein foldings within ER.
mechanism by which P58(IPK) functions to promote protein folding within the endoplasmic reticulum, determined from the crystal structure of P58(IPK)
renal injury inflicted by expression of the folding mutants was markedly enhanced by haploinsufficiency of the endoplasmic reticulum cochaperone p58(IPK).
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.
Insulin deficiency associated with the absence of P58(IPK) mimics beta-cell failure associated with type 1 and late-stage type 2 diabetes.
absence of P58(IPK) led to an increase in eIF2alpha phosphorylation and decreased influenza virus mRNA translation
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.
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
Selective and stable binding to misfolded proteins by P58's TPR-containing N-terminal domain, is reported.
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.
This gene encodes a protein with multiple tetratricopeptide repeat (TPR) motifs as well as the highly conserved J domain found in DNAJ chaperone family members. It is a member of the tetratricopeptide repeat family of proteins and acts as an inhibitor of the interferon-induced, dsRNA-activated protein kinase (PKR).
dnaJ homolog subfamily C member 3
, endoplasmic reticulum DnaJ protein 6
, interferon-induced, double-stranded RNA-activated protein kinase inhibitor
, protein kinase inhibitor of 58 kDa
, protein kinase inhibitor p58
, protein-kinase, interferon-inducible double stranded RNA dependent inhibitor
, DnaJ (Hsp40) homolog, subfamily C, member 3
, Interferon-induced, double-stranded RNA-activated protein kinase inhibitor
, TPR repeat-containing protein
, DnaJ (Hsp40) homolog, subfamily C, member 3A
, DnaJ (Hsp40) homolog, subfamily C, member 3B
, protein kinase, interferon inducible double stranded RNA dependent inhibitor