Molecular Biology of the Cell track citations

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


Originally published as MBC in Press, 10.1091/mbc.E07-07-0639 on February 13, 2008

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

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Materials
Right arrow All Versions of this Article:
E07-07-0639v1
19/4/1670    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Google Scholar
Right arrow Articles by López-Avilés, S.
Right arrow Articles by Aligue, R.
PubMed
Right arrow PubMed Citation
Right arrow Articles by López-Avilés, S.
Right arrow Articles by Aligue, R.

Activation of Srk1 by the Mitogen-activated Protein Kinase Sty1/Spc1 Precedes Its Dissociation from the Kinase and Signals Its Degradation

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

*Departament de Biologia Cellular, Universitat de Barcelona. Institut d'Investigacions Biomèdiques August Pi i Sunyer, 08036 Barcelona, Catalunya, Spain; {ddagger}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.


This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-07-0639) on February 13, 2008.

{dagger} 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.







Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2008 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.