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Activation of Srk1 by the Mitogen-activated Protein Kinase Sty1/Spc1 Precedes Its Dissociation from the Kinase and Signals Its Degradation
López Avilés, Sandra; Lambea Martínez, Eva; Moldón Vara, Alberto; Grande Robles, Maribel; Fajardo, Alba; Rodríguez-Gabriel, Miguel A.; Hidalgo Hernando, Elena; Aligué i Alemany, Rosa Maria
Universitat de Barcelona
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.
2012-06-01
Proteïnes quinases
Llevats
Cicle cel·lular
Protein kinases
Yeast
Cell cycle
cc-by-nc-sa, (c) López-Avilés et al., 2008
http://creativecommons.org/licenses/cc-by-nc-sa/3.0/es
Article
Article - Published version
American Society for Cell Biology
         

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