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The Srk1 protein kinase is a target for the Sty1 stress-activated MAPK in fission yeast

Lookup NU author(s): Professor Brian Morgan, Professor Janet Quinn


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The fission yeast stress-activated Sty1/Spc1 MAPK pathway responds to a similar range of stresses as do the mammalian p38 and SAPK/JNK MAPK pathways. In addition, sty1-cells are sterile and exhibit a G2 cell cycle delay, indicating additional roles of Sty1 in meiosis and cell cycle progression. To identify novel proteins involved in stress responses, a microarray analysis of the Schizosaccharomyces pombe genome was performed to find genes that are up-regulated following exposure to stress in a Sty1-dependent manner. One such gene identified, srk1+ (Sty1-regulated kinase 1), encodes a putative serine/threonine kinase homologous to mammalian calmodulin kinases. At the C terminus of Srk1 is a putative MAPK binding motif similar to that in the p38 substrates, MAPK-activated protein kinases 2 and 3. Indeed, we find that Srk1 is present in a complex with the Sty1 MAPK and is directly phosphorylated by Sty1. Furthermore, upon stress, Srk1 translocates from the cytoplasm to the nucleus in a process that is dependent on the Sty1 MAPK. Finally, we show that Srk1 has a role in regulating meiosis in fission yeast; following nitrogen limitation, srk1-cells enter meiosis significantly faster than wild-type cells and overexpression of srk1+ inhibits the nitrogen starvation-induced arrest in G1.

Publication metadata

Author(s): Morgan BA; Quinn J; Smith DA; Mark Toone W; Chen D; Bahler J; Jones N

Publication type: Article

Publication status: Published

Journal: Journal of Biological Chemistry

Year: 2002

Volume: 277

Issue: 36

Pages: 33411-33421

ISSN (print): 0021-9258

ISSN (electronic): 1083-351X

Publisher: American Society for Biochemistry and Molecular Biology, Inc.


DOI: 10.1074/jbc.M204593200

PubMed id: 12080074


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Funder referenceFunder name
077118Wellcome Trust
A6517Cancer Research UK