Regulation of MAP Kinase Signaling Modules by Scaffold Proteins in Mammals

Annual Review of Cell and Developmental Biology

Vol. 19:91-118 (Volume publication date November 2003)
First published online as a Review in Advance on July 23, 2003
https://doi.org/10.1146/annurev.cellbio.19.111401.091942

Abstract

AbstractThe mitogen-activated protein kinase (MAPK) group of serine/threonine protein kinases mediates the response of cells to many extracellular stimuli such as cytokines and growth factors. These protein kinases include the extracellular signal-regulated protein kinases (ERK) and two stress-activated protein kinases (SAPK), the c-Jun N-terminal kinases (JNK), and the p38 MAPK. The enzymes are evolutionarily conserved and are activated by a common mechanism that involves a protein kinase cascade. Scaffold proteins have been proposed to interact with MAPK pathway components to create a functional signaling module and to control the specificity of signal transduction. Here we critically evaluate the evidence that supports a physiologically relevant role of MAPK scaffold proteins in mammals.

Footnotes:

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