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Calcium depletion from the endoplasmic reticulum inhibits
protein synthesis and correlates with increased phosphorylation of the
Volume 270,
Number 28,
Issue of July 14, pp. 16619-16624, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
subunit of eukaryotic initiation factor 2 (eIF-2) by a
mechanism that does not require ongoing protein synthesis. To elucidate
whether protein synthesis inhibition requires eIF-2
phosphorylation and whether eIF-2 phosphorylation is mediated by
the double-stranded RNA-dependent protein kinase (PKR), we studied
protein synthesis in response to calcium depletion mediated by calcium
ionophore A23187 in cell lines overexpressing wild-type eIF-2, a
mutant eIF-2 (S51A) that is resistant to phosphorylation, or a
dominant negative mutant PKR (K296P in catalytic subdomain II).
Expression of either mutant eIF-2 or mutant PKR partially
protected NIH3T3 cells from inhibition of protein synthesis upon A23187
treatment. In contrast, overexpression of wild-type PKR increased
sensitivity to protein synthesis inhibition mediated by A23187
treatment. In a COS-1 monkey cell transient transfection system,
increased eIF-2 phosphorylation in response to A23187 treatment
was inhibited by expression of the dominant negative PKR mutant.
Overexpression of the PKR regulatory RNA binding domain, independent of
the PKR catalytic domain, was sufficient to inhibit increased
phosphorylation of eIF-2 upon A23187 treatment. In addition,
overexpression of the HIV TAR RNA binding protein also inhibited
eIF-2 phosphorylation upon A23187 treatment. Taken together, our
data show that calcium depletion activates PKR to phosphorylate
eIF-2, and this activation is likely mediated through the PKR RNA
binding domain.
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