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Overview
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MAPKAPK5 is a member of the serine/threonine kinase family that responds to cellular stress and proinflammatory cytokines. MAPKAPK5 is activated through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. MAPKAPK5 is activated in HeLa cells in response to cellular stress and proinflammatory cytokines. MAPKAPK5 activity is regulated by p38-alpha and p38-beta both in vitro and in vivo, and thr-182 is the regulatory phosphorylation site of MAPKAPK5. In vitro, MAPKAPK5 kinase phosphorylates heat shock protein HSP27 at its physiologically relevant sites.
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