Translational control by TOR and TAP42 through dephosphorylation of eIF2α kinase GCN2
作者： V. A. Cherkasova
DOI: 10.1101/GAD.1069003
关键词:
摘要: Yeast protein kinase GCN2 stimulates the translation of transcriptional activator GCN4 by phosphorylating eIF2α in response to amino acid starvation. Kinase activation requires binding uncharged tRNA a histidyl synthetase-related domain GCN2. Phosphorylation serine 577 (Ser 577) another vivo inhibits function rich medium reducing activity. We show that rapamycin phosphorylation GCN2, with attendant induction translation, while Ser nonstarved cells. The alanine (Ala mutation (S577A) dampened effects on and suggesting involves dephosphorylation. Rapamycin regulates inhibiting TOR pathway. Rapamycin-induced dephosphorylation 577, phosphorylation, all involve TAP42, regulator type 2A-related phosphatases. Our results add new dimension regulation synthesis proteins demonstrate cross-talk between two major pathways for nutrient control gene expression yeast.
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