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    H2O2 stress-specific regulation of S. pombe MAPK Sty1 by mitochondrial protein phosphatase Ptc4.

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    Authors
    Di, Yujun
    Holmes, Emily J
    Butt, Amna
    Dawson, Keren
    Mironov, A
    Kotiadis, V N
    Gourlay, C W
    Jones, Nic
    Wilkinson, Caroline R M
    Affiliation
    Cell Regulation Group, Paterson Institute for Cancer Research, University of Manchester, Manchester, UK.
    Issue Date
    2012-02-01
    
    Metadata
    Show full item record
    Abstract
    In fission yeast, the stress-activated MAP kinase, Sty1, is activated via phosphorylation upon exposure to stress and orchestrates an appropriate response. Its activity is attenuated by either serine/threonine PP2C or tyrosine phosphatases. Here, we found that the PP2C phosphatase, Ptc4, plays an important role in inactivating Sty1 specifically upon oxidative stress. Sty1 activity remains high in a ptc4 deletion mutant upon H(2)O(2) but not under other types of stress. Surprisingly, Ptc4 localizes to the mitochondria and is targeted there by an N-terminal mitochondrial targeting sequence (MTS), which is cleaved upon import. A fraction of Sty1 also localizes to the mitochondria suggesting that Ptc4 attenuates the activity of a mitochondrial pool of this MAPK. Cleavage of the Ptc4 MTS is greatly reduced specifically upon H(2)O(2), resulting in the full-length form of the phosphatase; this displays a stronger interaction with Sty1, thus suggesting a novel mechanism by which the negative regulation of MAPK signalling is controlled and providing an explanation for the oxidative stress-specific nature of the regulation of Sty1 by Ptc4.
    Citation
    H2O2 stress-specific regulation of S. pombe MAPK Sty1 by mitochondrial protein phosphatase Ptc4. 2012, 31 (3):563-75 EMBO J.
    Journal
    EMBO Journal
    URI
    http://hdl.handle.net/10541/216289
    DOI
    10.1038/emboj.2011.438
    PubMed ID
    22139357
    Type
    Article
    Language
    en
    ISSN
    1460-2075
    ae974a485f413a2113503eed53cd6c53
    10.1038/emboj.2011.438
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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