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dc.contributor.authorDi, Yujun
dc.contributor.authorHolmes, Emily J
dc.contributor.authorButt, Amna
dc.contributor.authorDawson, Keren
dc.contributor.authorMironov, A
dc.contributor.authorKotiadis, V N
dc.contributor.authorGourlay, C W
dc.contributor.authorJones, Nic
dc.contributor.authorWilkinson, Caroline R M
dc.date.accessioned2012-03-22T13:14:59Z
dc.date.available2012-03-22T13:14:59Z
dc.date.issued2012-02-01
dc.identifier.citationH2O2 stress-specific regulation of S. pombe MAPK Sty1 by mitochondrial protein phosphatase Ptc4. 2012, 31 (3):563-75 EMBO J.en_GB
dc.identifier.issn1460-2075
dc.identifier.pmid22139357
dc.identifier.doi10.1038/emboj.2011.438
dc.identifier.urihttp://hdl.handle.net/10541/216289
dc.description.abstractIn 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.
dc.language.isoenen
dc.rightsArchived with thanks to The EMBO journalen_GB
dc.subject.meshHydrogen Peroxide
dc.subject.meshMitochondria
dc.subject.meshMitogen-Activated Protein Kinases
dc.subject.meshPhosphoprotein Phosphatases
dc.subject.meshSchizosaccharomyces pombe Proteins
dc.titleH2O2 stress-specific regulation of S. pombe MAPK Sty1 by mitochondrial protein phosphatase Ptc4.en
dc.typeArticleen
dc.contributor.departmentCell Regulation Group, Paterson Institute for Cancer Research, University of Manchester, Manchester, UK.en_GB
dc.identifier.journalEMBO Journalen_GB
html.description.abstractIn 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.


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