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• W2107149701 abstract "A structurally distinct subfamily of ten dual-specificity (Thr/Tyr) protein phosphatases is responsible for the regulated dephosphorylation and inactivation of mitogen-activated protein kinase (MAPK) family members in mammals. These MAPK phosphatases (MKPs) interact specifically with their substrates through a modular kinase-interaction motif (KIM) located within the N-terminal non-catalytic domain of the protein. In addition, MAPK binding is often accompanied by enzymatic activation of the C-terminal catalytic domain, thus ensuring specificity of action. Despite our knowledge of the biochemical and structural basis for the catalytic mechanism of the MKPs, we know much less about their regulation and physiological functions in mammalian cells and tissues. However, recent studies employing a range of model systems have begun to reveal essential non-redundant roles for the MKPs in determining the outcome of MAPK signalling in a variety of physiological contexts. These include development, immune system function, metabolic homeostasis and the regulation of cellular stress responses. Interestingly, these functions may reflect both restricted subcellular MKP activity and changes in the levels of signalling through multiple MAPK pathways." @default.
• W2107149701 created "2016-06-24" @default.
• W2107149701 creator A5033321035 @default.
• W2107149701 creator A5091622396 @default.
• W2107149701 date "2006-11-15" @default.
• W2107149701 modified "2023-10-10" @default.
• W2107149701 title "Diverse physiological functions for dual-specificity MAP kinase phosphatases" @default.
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• W2107149701 doi "https://doi.org/10.1242/jcs.03266" @default.
• W2107149701 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17093265" @default.
• W2107149701 hasPublicationYear "2006" @default.
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