MAP kinase activation during heat shock in quiescent and exponentially growing mammalian cells.
In numerous cases of signal transduction, the mitogen-activated protein kinases (MAP kinases) or extracellular regulated kinases (ERKs) are found to be activated by phosphorylations which result in electrophoretic mobility changes. Activities of MAP kinases in cytosolic extracts can also be monitored by the capacity of such extracts to phosphorylate myelin basic protein. These two assays were used to demonstrate that MAP kinases were rapidly activated during heat shock of both quiescent and exponentially growing mammalian (hamster, rat, mouse and human) cells. Thus, the MAP kinase cascade is likely to also ensure heat-shock signal transduction and contribute to the regulation of the complex array of metabolic changes designated as the heat-shock response.
Génétique Moléculaire, URA CNRS 1302, Paris, France.
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D000818:Animals; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D002455:Cell Division; D002474:Cell-Free System; D002478:Cells, Cultured; D006224:Cricetinae; D003412:Cricetulus; D003600:Cytosol / Q000201:enzymology; D004789:Enzyme Activation; D006358:Hot Temperature; D006801:Humans; D048052:Mitogen-Activated Protein Kinase 3; D020928:Mitogen-Activated Protein Kinases; D011494:Protein Kinases / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases; D051381:Rats; D015398:Signal Transduction
D011494:Protein Kinases; D017346:Protein Serine-Threonine Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D048052:Mitogen-Activated Protein Kinase 3; D020928:Mitogen-Activated Protein Kinases