NDLI: Regulation of starvation- and virus-induced autophagy by the eIF2alpha kinase signaling pathway.

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Regulation of starvation- and virus-induced autophagy by the eIF2alpha kinase signaling pathway.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Jiang, Wenxia Tallóczy, Zsolt Leib, David A. Kaufman, Randal J. Scheuner, Donalyn Virgin, Herbert W. Eskelinen, Eeva-liisa Levine, Beth
Description	Author Affiliation: Tallóczy Z ( Department of Medicine, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.);
Abstract	The eIF2alpha kinases are a family of evolutionarily conserved serine/threonine kinases that regulate stress-induced translational arrest. Here, we demonstrate that the yeast eIF2alpha kinase, GCN2, the target phosphorylation site of Gcn2p, Ser-51 of eIF2alpha, and the eIF2alpha-regulated transcriptional transactivator, GCN4, are essential for another fundamental stress response, starvation-induced autophagy. The mammalian IFN-inducible eIF2alpha kinase, PKR, rescues starvation-induced autophagy in GCN2-disrupted yeast, and pkr null and Ser-51 nonphosphorylatable mutant eIF2alpha murine embryonic fibroblasts are defective in autophagy triggered by herpes simplex virus infection. Furthermore, PKR and eIF2alpha 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 eIF2alpha kinase pathway that is targeted by viral virulence gene products.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	1
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DNA-Binding Proteins Fungal Proteins Physiology Phagocytosis Protein Kinases Saccharomyces Cerevisiae Proteins Signal Transduction EIF-2 Kinase Metabolism Animals Binding Sites Blotting, Western Cells, Cultured Fibroblasts Immunohistochemistry Mice Mutation Phosphorylation Protein Binding Serine Chemistry Simplexvirus Pathogenicity Time Factors Transcriptional Activation Viral Proteins Genetics Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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