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M212074200v1
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Papers In Press, published online ahead of print February 24, 2003
J. Biol. Chem, 10.1074/jbc.M212074200
Submitted on November 26, 2002
Revised on February 11, 2003
Accepted on February 24, 2003

P58IPK, a novel ER stress-inducible protein and potential negative regulator of eIF2a signaling

Rika van Huizen, Jennifer L. Martindale, Myriam Gorospe, and Nikki J. Holbrook

Box 12, LCMB, NIA, National Institutes of Health, Baltimore, MD 21228

Corresponding Author: huizenri{at}grc.nia.nih.gov

The unfolded protein response (UPR), which is activated in response to the loss of ER Ca2+ homeostasis and/or the accumulation of misfolded, unassembled, or aggregated proteins in the ER lumen, involves both transcriptional and translational regulation. In the current studies we sought to identify novel ER stress-induced genes by conducting microarray analysis on tunicamycin-treated cells. We identified P58IPK, an inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR), as induced during ER stress. Additional studies suggested that p58IPK induction was mediated via ATF6 and that P58IPK played a role in down-regulating the activity of the PERK/eIF2a/ATF4 pathway. Modulation of P58IPK levels altered the phosphorylation status of eIF2a, and thereby affected expression of its downstream targets, ATF4 and Gadd153. Overexpression of P58IPK inhibited eIF2a phosphorylation and reduced ATF4 and Gadd153 protein accumulation, while silencing of P58IPK expression enhanced PERK and eIF2a phosphorylation and increased ATF4 and Gadd153 accumulation. These findings implicate P58IPK as an important component of a negative feedback loop used by the cell to inhibit eIF2a signaling, and thus attenuate the UPR.


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