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dc.contributor.authorSmith, Deborah A
dc.contributor.authorToone, W Mark
dc.contributor.authorChen, Dongrong
dc.contributor.authorBahler, Jurg
dc.contributor.authorJones, Nic
dc.contributor.authorMorgan, Brian A
dc.contributor.authorQuinn, Janet
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).
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
html.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).


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