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Vol. 19, Issue 4, 1670-1679, April 2008

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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

Sandra López-Avilés^*,, Eva Lambea^*,, Alberto Moldón, Maribel Grande^*,, Alba Fajardo^*, Miguel A. Rodríguez-Gabriel^||, Elena Hidalgo, and Rosa Aligue^*

*Departament de Biologia Cellular, Universitat de Barcelona. Institut d'Investigacions Biomèdiques August Pi i Sunyer, 08036 Barcelona, Catalunya, Spain; Departament de Ciències Experimentals i de la Salut, Universitat Pompeu Fabra. 08003 Barcelona, Catalunya, Spain; and ^||Departamento de Microbiologia II. Universidad Complutense, 28040 Madrid, Spain

Submitted July 5, 2007; Revised January 9, 2008; Accepted February 1, 2008
Monitoring Editor: Daniel Lew

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.

These authors contributed equally to this work.

Present address: Institut de Biologia Molecular de Barcelona (IBMB-CSIC), Parc Científic de Barcelona, C/Joseph Samitier 1-5, 08028 Barcelona, Catalunya, Spain.

Address correspondence to: Rosa Aligue (aliguerosa{at}ub.edu).

Abbreviations used: GST, glutathione S-transferase.

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