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Regulation of starvation- and virus-induced autophagy by the eIF2α kinase signaling pathway
Open accessAbstract
The eIF2α kinases are a family of evolutionarily conserved serine/threonine kinases that regulate stress-induced translational arrest. Here, we demonstrate that the yeast eIF2α kinase, GCN2 , the target phosphorylation site of Gcn2p, Ser-51 of eIF2α, and the eIF2α-regulated transcriptional transactivator, GCN4 , are essential for another fundamental stress response, starvation-induced autophagy. The mammalian IFN-inducible eIF2α kinase, PKR, rescues starvation-induced autophagy in GCN2 -disrupted yeast, and pkr null and Ser-51 nonphosphorylatable mutant eIF2α murine embryonic fibroblasts are defective in autophagy triggered by herpes simplex virus infection. Furthermore, PKR and eIF2α 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 eIF2α kinase pathway that is targeted by viral virulence gene products.
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Self-citation(2012) · PubMed
Metadata
- Authors
- Tallóczy, Z., Jiang, W., Virgin, H. W., Leib, D. A., Scheuner, D., Kaufman, R. J., Eskelinen, E.-L., & Levine, B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2001-12-26
- Volume
- 99
- Issue
- 1
- Pages
- 190-195
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2001467419
- Cited by
- 741
- References
- 3
- FWCI
- 10.46
- Type
- journal article
- Language
- en
- Open access
- green
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