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Tallóczy, Zsolt; Jiang, Wenxia; Virgin, Herbert W.; Leib, David A.; Scheuner, Donalyn; Kaufman, Randal J.; Eskelinen, Eeva-Liisa; Levine, Beth
Proceedings of the National Academy of Sciences - PNAS, 01/2002, Volume: 99, Issue: 1Journal Article
The elF2α kinases are a family of evolutionarily conserved serine/threonine kinases that regulate stress-induced translational arrest. Here, we demonstrate that the yeast elF2α kinase, GCN2, the target phosphorylation site of Gcn2p, Ser-51 of elF2α, and the elF2α-regulated transcriptional transactivator, GCN4, are essential for another fundamental stress response, starvation-induced autophagy. The mammalian IFN-inducible elF2α kinase, PKR, rescues starvation-induced autophagy in GCN2-disrupted yeast, and pkr null and Ser-51 nonphosphorylatable mutant elF2α murine embryonic fibroblasts are defective in autophagy triggered by herpes simplex virus infection. Furthermore, PKR and elF2α Ser-51-dependent autophagy is antagonized by the herpes simplex virus neurovirulence protein, ICP34.5. Thus, autophagy is a novel evolutionarily conserved function of the elF2α kinase pathway that is targeted by viral virulence gene products.
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