Sch9 Is a Major Target of TORC1 in Saccharomyces cerevisiae
| Autor: | Olivier Deloche, Alexandre Soulard, Claudio De Virgilio, James R. Broach, Robbie Loewith, Dorothea Anrather, Howard Riezman, Alexandre Huber, Gustav Ammerer, Michael N. Hall, Soyeon I. Lippman, Valeria Wanke, Jörg Urban, Debdyuti Mukhopadhyay |
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| Rok vydání: | 2007 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Protein Kinases/chemistry/genetics/metabolism Saccharomyces cerevisiae Genes Fungal TORC1 signaling P70-S6 Kinase 1 Biology Protein Serine-Threonine Kinases mTORC2 Regulon Resting Phase Cell Cycle G0 Phase Osmotic Pressure ddc:570 TOR complex Amino Acid Sequence Phosphorylation Protein kinase B Molecular Biology ddc:616 Sirolimus Recombinant Proteins/chemistry/genetics/metabolism Binding Sites Kinase Vacuoles/metabolism Temperature Saccharomyces cerevisiae Proteins/chemistry/metabolism Sirolimus/pharmacology Cell Biology biology.organism_classification Saccharomyces cerevisiae/cytology/genetics/metabolism Recombinant Proteins Oxidative Stress Biochemistry Amino Acid Substitution Multiprotein Complexes Protein Biosynthesis ddc:540 Vacuoles Mutagenesis Site-Directed Protein-Serine-Threonine Kinases/chemistry/metabolism Protein Kinases |
| Zdroj: | Molecular Cell, Vol. 26, No 5 (2007) pp. 663-74 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/j.molcel.2007.04.020 |
| Popis: | The Target of Rapamycin (TOR) protein is a Ser/Thr kinase that functions in two distinct multiprotein complexes: TORC1 and TORC2. These conserved complexes regulate many different aspects of cell growth in response to intracellular and extracellular cues. Here we report that the AGC kinase Sch9 is a substrate of yeast TORC1. Six amino acids in the C terminus of Sch9 are directly phosphorylated by TORC1. Phosphorylation of these residues is lost upon rapamycin treatment as well as carbon or nitrogen starvation and transiently reduced following application of osmotic, oxidative, or thermal stress. TORC1-dependent phosphorylation is required for Sch9 activity, and replacement of residues phosphorylated by TORC1 with Asp/Glu renders Sch9 activity TORC1 independent. Sch9 is required for TORC1 to properly regulate ribosome biogenesis, translation initiation, and entry into G0 phase, but not expression of Gln3-dependent genes. Our results suggest that Sch9 functions analogously to the mammalian TORC1 substrate S6K1 rather than the mTORC2 substrate PKB/Akt. |
| Databáze: | OpenAIRE |
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