Activation of Srk1 by the Mitogen-activated Protein Kinase Sty1/Spc1 Precedes Its Dissociation from the Kinase and Signals Its Degradation
| Autor: | Eva Lambea, Alberto Moldón, Sandra López-Avilés, Rosa Aligué, Maribel Grande, Elena Hidalgo, Alba Fajardo, Miguel A. Rodríguez-Gabriel |
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| Přispěvatelé: | Universitat de Barcelona |
| Předmět: |
Threonine
Proteasome Endopeptidase Complex MAP Kinase Signaling System Recombinant Fusion Proteins Active Transport Cell Nucleus Cell Cycle Proteins Biology Mitogen-activated protein kinase kinase Cell cycle Cicle cel·lular Models Biological MAP2K7 Fungal Proteins Protein kinases Gene Expression Regulation Fungal Enzyme Stability Schizosaccharomyces ASK1 Phosphorylation Molecular Biology Cyclin-dependent kinase 1 MAP kinase kinase kinase ras-GRF1 Cyclin-dependent kinase 2 Cell Cycle Cell Biology Articles Yeast Cell biology Protein Structure Tertiary Enzyme Activation Proteïnes quinases Amino Acid Substitution biology.protein Mutagenesis Site-Directed Cyclin-dependent kinase 9 Schizosaccharomyces pombe Proteins Cyclin-dependent kinase 7 Mitogen-Activated Protein Kinases Llevats Signal Transduction |
| Zdroj: | Recercat. Dipósit de la Recerca de Catalunya instname Dipòsit Digital de la UB Universidad de Barcelona |
| Popis: | Control of cell cycle progression by stress-activated protein kinases (SAPKs) is essential for cell adaptation to extracellular stimuli. The Schizosaccharomyces pombe SAPK Sty1/Spc1 orchestrates general changes in gene expression in response to diverse forms of cytotoxic stress. Here we show that Sty1/Spc1 is bound to its target, the Srk1 kinase, when the signaling pathway is inactive. In response to stress, Sty1/Spc1 phosphorylates Srk1 at threonine 463 of the regulatory domain, inducing both activation of Srk1 kinase, which negatively regulates cell cycle progression by inhibiting Cdc25, and dissociation of Srk1 from the SAPK, which leads to Srk1 degradation by the proteasome. |
| Databáze: | OpenAIRE |
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