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Activation of the Mitogen-Activated Protein Kinase Pathways by Heat Shock

Sonia Dorion and Jacques Landry
Cell Stress & Chaperones
Vol. 7, No. 2 (Apr., 2002), pp. 200-206
Published by: Cell Stress Society International in partnership with Springer
Stable URL: http://www.jstor.org/stable/1602044
Page Count: 7
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Activation of the Mitogen-Activated Protein Kinase Pathways by Heat Shock
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Abstract

In addition to inducing new transcriptional activities that lead within a few hours to the accumulation of heat shock proteins (Hsps), heat shock activates within minutes the major signaling transduction pathways involving mitogen-activated protein kinases, extracellular signal-regulated kinase, stress-activated protein kinase 1 (SAPK1)-c-Jun N-terminal kinase, and SAPK2-p38. These kinases are involved in both survival and death pathways in response to other stresses and may, therefore, contribute significantly to the heat shock response. In the case of p38, the activation leads to the phosphorylation and activation of one of the Hsps, Hsp27. Phosphorylation occurs very early during stress, is tightly regulated, and results from the triggering of a highly specific heat shock-sensing pathway.

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