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

2.50
Hdl Handle:
http://hdl.handle.net/10541/84048
Title:
The Srk1 protein kinase is a target for the Sty1 stress-activated MAPK in fission yeast.
Authors:
Smith, Deborah A; Toone, W Mark; Chen, Dongrong; Bahler, Jurg; Jones, Nic; Morgan, Brian A; Quinn, Janet
Abstract:
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 G(2) 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 G(1).
Affiliation:
School of Biochemistry and Genetics, Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, United Kingdom.
Citation:
The Srk1 protein kinase is a target for the Sty1 stress-activated MAPK in fission yeast. 2002, 277 (36):33411-21 J. Biol. Chem.
Journal:
The Journal of Biological Chemistry
Issue Date:
6-Sep-2002
URI:
http://hdl.handle.net/10541/84048
DOI:
10.1074/jbc.M204593200
PubMed ID:
12080074
Type:
Article
Language:
en
ISSN:
0021-9258
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorSmith, Deborah Aen
dc.contributor.authorToone, W Marken
dc.contributor.authorChen, Dongrongen
dc.contributor.authorBahler, Jurgen
dc.contributor.authorJones, Nicen
dc.contributor.authorMorgan, Brian Aen
dc.contributor.authorQuinn, Janeten
dc.date.accessioned2009-10-12T12:25:46Z-
dc.date.available2009-10-12T12:25:46Z-
dc.date.issued2002-09-06-
dc.identifier.citationThe Srk1 protein kinase is a target for the Sty1 stress-activated MAPK in fission yeast. 2002, 277 (36):33411-21 J. Biol. Chem.en
dc.identifier.issn0021-9258-
dc.identifier.pmid12080074-
dc.identifier.doi10.1074/jbc.M204593200-
dc.identifier.urihttp://hdl.handle.net/10541/84048-
dc.description.abstractThe 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 G(2) 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 G(1).en
dc.language.isoenen
dc.subject.meshActive Transport, Cell Nucleus-
dc.subject.meshAmino Acid Motifs-
dc.subject.meshAmino Acid Sequence-
dc.subject.meshBlotting, Western-
dc.subject.meshCell Nucleus-
dc.subject.meshFlow Cytometry-
dc.subject.meshFungal Proteins-
dc.subject.meshG1 Phase-
dc.subject.meshG2 Phase-
dc.subject.meshHydrogen Peroxide-
dc.subject.meshMAP Kinase Signaling System-
dc.subject.meshMeiosis-
dc.subject.meshMitogen-Activated Protein Kinase Kinases-
dc.subject.meshMitogen-Activated Protein Kinases-
dc.subject.meshMolecular Sequence Data-
dc.subject.meshNitrogen-
dc.subject.meshOligonucleotide Array Sequence Analysis-
dc.subject.meshPhenotype-
dc.subject.meshPhosphorylation-
dc.subject.meshPlasmids-
dc.subject.meshPrecipitin Tests-
dc.subject.meshProtein Binding-
dc.subject.meshProtein Structure, Tertiary-
dc.subject.meshProtein Transport-
dc.subject.meshProtein-Serine-Threonine Kinases-
dc.subject.meshSaccharomyces cerevisiae Proteins-
dc.subject.meshSchizosaccharomyces-
dc.subject.meshSchizosaccharomyces pombe Proteins-
dc.subject.meshSequence Homology, Amino Acid-
dc.subject.meshTime Factors-
dc.subject.meshUp-Regulation-
dc.titleThe Srk1 protein kinase is a target for the Sty1 stress-activated MAPK in fission yeast.en
dc.typeArticleen
dc.contributor.departmentSchool of Biochemistry and Genetics, Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, United Kingdom.en
dc.identifier.journalThe Journal of Biological Chemistryen

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