The regulation of MAP kinase signalling by dual-specificity protein phosphatases

Published on March 16, 2011   49 min

Other Talks in the Series: Protein Phosphorylation

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Hi, my name's Steve Keyse, and I'm based at the University of Dundee in Scotland; And the subject of my talk today, is "The Regulation of Mitogen-activated Protein Kinase Signalling by Dual-Specificity Protein Phosphatases.
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This next slide shows an overview, the mitogen and stress-activated protein kinase signalling cascades in mammalian cells. These highly conserve signal transduction pathways, serve to respond to a series of environmental cues which range from growth factors and hormones, through to cellular stresses such as pro-inflammatory cytokines and DNA damaging agents, and elicit a wide variety of physiological responses in cells, which range from increases in the rate of cell growth or cell differentiation, changes in morphology and motility, mediation of inflammatory responses, cell cycle arrest, and even cell death. These pathways are divided into three major families: the so-called classical Ras-MAP kinase pathway which is largely responsible for the response to growth factors and hormones, and is thought primarily to influence cell growth, differentiation and survival. There are two so-called stress-activated MAP kinase pathways exemplified by the c-Jun amino-terminal kinases or JNKs, and the p38 MAP kinases, which respond primarily to cellular stress and pro-inflammatory cytokines, and are thought to be responsible for exit from the cell cycle, and responses to damage such as cell death.
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The regulation of MAP kinase signalling by dual-specificity protein phosphatases

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