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• W2080642736 startingPage "2387" @default.
• W2080642736 abstract "Stress signals elicit a wide variety of cellular responses, many of which converge on the phosphorylation of JNK and p38 kinases, the activation of which has been well-characterized. How these kinases are switched off by dephosphorylation is not well understood. Here we describe how diverse cellular stresses affect differently the stability and activity of a JNK-inactivating dual-specificity threonine-tyrosine phosphatase M3/6. Both anisomycin and arsenite activate the JNK pathway and, in addition, inactivate the M3/6 phosphatase. However, while anisomycin treatment of cells leads to M3/6 protein degradation, arsenite appears to inactivate M3/6 directly. These results might have implications for the mechanism of tumour promotion by arsenic." @default.
• W2080642736 created "2016-06-24" @default.
• W2080642736 creator A5058973407 @default.
• W2080642736 creator A5083316854 @default.
• W2080642736 date "2002-04-04" @default.
• W2080642736 modified "2023-09-27" @default.
• W2080642736 title "Differential effects of stress stimuli on a JNK-inactivating phosphatase" @default.
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• W2080642736 doi "https://doi.org/10.1038/sj.onc.1205309" @default.
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