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Publication Detail
The Srk1 protein kinase is a target for the Sty1 stress-activated MAPK in fission yeast.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Smith DA, Toone WM, Chen D, Bahler J, Jones N, Morgan BA, Quinn J
  • Publication date:
    06/09/2002
  • Pagination:
    33411, 33421
  • Journal:
    J Biol Chem
  • Volume:
    277
  • Issue:
    36
  • Status:
    Published
  • Country:
    United States
  • Print ISSN:
    0021-9258
  • PII:
    M204593200
  • Language:
    eng
  • Keywords:
    Active Transport, Cell Nucleus, Amino Acid Motifs, Amino Acid Sequence, Blotting, Western, Cell Nucleus, Flow Cytometry, Fungal Proteins, G1 Phase, G2 Phase, Hydrogen Peroxide, MAP Kinase Signaling System, Meiosis, Mitogen-Activated Protein Kinase Kinases, Mitogen-Activated Protein Kinases, Molecular Sequence Data, Nitrogen, Oligonucleotide Array Sequence Analysis, Phenotype, Phosphorylation, Plasmids, Precipitin Tests, Protein Binding, Protein Structure, Tertiary, Protein Transport, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Sequence Homology, Amino Acid, Time Factors, Up-Regulation
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).
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