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Evidence for a novel MAPKKK-independent pathway controlling the stress activated Sty1/Spc1 MAP kinase in fission yeast.
J Cell Sci. 1998 Sep; 111 (Pt 18):2799-807.JC

Abstract

The fission yeast Sty1/Spc1 MAP kinase, like the mammalian JNK/SAPK and p38/CSBP1 kinases, is activated by a range of environmental insults including osmotic stress, hydrogen peroxide, heat shock, UV light and the protein synthesis inhibitor anisomycin. Sty1 is activated by a single MAPKK, Wis1. We demonstrate that the conserved MAPKKK phosphorylation sites Ser 469 and Thr 473 in the catalytic domain of Wis1 are normally essential for Sty1 activation. However, when mildly overexpressed, a mutant Wis1 kinase lacking these conserved phosphorylation sites is able to support stress inducible gene expression and activation of the Sty1 MAP kinase in response to an oxidative or osmotic stress or to a mild heat shock. We show that phosphorylation and activation of Sty1 under these conditions is not due to inactivation of the Pyp1 MAP kinase phosphatase. These results reveal a novel MAPKKK-independent pathway by which the Wis1 MAPKK can activate the Sty1 MAPK in response to stress in fission yeast.

Authors+Show Affiliations

Division of Yeast Genetics, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9718372

Citation

Shieh, J C., et al. "Evidence for a Novel MAPKKK-independent Pathway Controlling the Stress Activated Sty1/Spc1 MAP Kinase in Fission Yeast." Journal of Cell Science, vol. 111 (Pt 18), 1998, pp. 2799-807.
Shieh JC, Martin H, Millar JB. Evidence for a novel MAPKKK-independent pathway controlling the stress activated Sty1/Spc1 MAP kinase in fission yeast. J Cell Sci. 1998;111 (Pt 18):2799-807.
Shieh, J. C., Martin, H., & Millar, J. B. (1998). Evidence for a novel MAPKKK-independent pathway controlling the stress activated Sty1/Spc1 MAP kinase in fission yeast. Journal of Cell Science, 111 (Pt 18), 2799-807.
Shieh JC, Martin H, Millar JB. Evidence for a Novel MAPKKK-independent Pathway Controlling the Stress Activated Sty1/Spc1 MAP Kinase in Fission Yeast. J Cell Sci. 1998;111 (Pt 18):2799-807. PubMed PMID: 9718372.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Evidence for a novel MAPKKK-independent pathway controlling the stress activated Sty1/Spc1 MAP kinase in fission yeast. AU - Shieh,J C, AU - Martin,H, AU - Millar,J B, PY - 1998/8/27/pubmed PY - 1998/8/27/medline PY - 1998/8/27/entrez SP - 2799 EP - 807 JF - Journal of cell science JO - J Cell Sci VL - 111 (Pt 18) N2 - The fission yeast Sty1/Spc1 MAP kinase, like the mammalian JNK/SAPK and p38/CSBP1 kinases, is activated by a range of environmental insults including osmotic stress, hydrogen peroxide, heat shock, UV light and the protein synthesis inhibitor anisomycin. Sty1 is activated by a single MAPKK, Wis1. We demonstrate that the conserved MAPKKK phosphorylation sites Ser 469 and Thr 473 in the catalytic domain of Wis1 are normally essential for Sty1 activation. However, when mildly overexpressed, a mutant Wis1 kinase lacking these conserved phosphorylation sites is able to support stress inducible gene expression and activation of the Sty1 MAP kinase in response to an oxidative or osmotic stress or to a mild heat shock. We show that phosphorylation and activation of Sty1 under these conditions is not due to inactivation of the Pyp1 MAP kinase phosphatase. These results reveal a novel MAPKKK-independent pathway by which the Wis1 MAPKK can activate the Sty1 MAPK in response to stress in fission yeast. SN - 0021-9533 UR - https://www.unboundmedicine.com/medline/citation/9718372/Evidence_for_a_novel_MAPKKK_independent_pathway_controlling_the_stress_activated_Sty1/Spc1_MAP_kinase_in_fission_yeast_ L2 - http://jcs.biologists.org/cgi/pmidlookup?view=long&pmid=9718372 DB - PRIME DP - Unbound Medicine ER -