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• W2066756921 abstract "Protein kinase R (PKR), a regulator of translation in mammalian cells, possesses two ds-RNA binding domains responsible for kinase activation. Protein kinase Z (PKZ), a PKR-like kinase present in fish, possesses two Z-DNA binding domains. A complementation strategy with cells stably deficient in PKR was used to compare the functions of PKR and PKZ. We found reporter expression was inhibited by wildtype (WT) PKR but not by either catalytic (K296R) or RNA-binding (K64E) mutants. PKZ, like PKR, more potently inhibited 5′ cap-dependent compared to IRES-dependent reporter expression. However, in contrast to PKR-expressing cells, phosphorylation of initiation factor eIF2α was not detectably increased in PKZ-expressing cells. Furthermore, virus-induced stress granule formation was observed in PKR-deficient cells complemented with WT PKR but not K296R mutant PKR or WT PKZ. These results suggest that PKR and PKZ function by distinguishable mechanisms to modulate host responses including protein synthesis inhibition and stress granule formation." @default.
• W2066756921 created "2016-06-24" @default.
• W2066756921 creator A5031909976 @default.
• W2066756921 creator A5071740906 @default.
• W2066756921 date "2013-08-01" @default.
• W2066756921 modified "2023-09-29" @default.
• W2066756921 title "RNA-dependent protein kinase PKR and the Z-DNA binding orthologue PKZ differ in their capacity to mediate initiation factor eIF2α-dependent inhibition of protein synthesis and virus-induced stress granule formation" @default.
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• W2066756921 doi "https://doi.org/10.1016/j.virol.2013.04.020" @default.
• W2066756921 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3700635" @default.
• W2066756921 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23706307" @default.
• W2066756921 hasPublicationYear "2013" @default.
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