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Updated: Aug 17, 2026

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Published on: November 8, 2006
Regulation of MAP kinase signaling modules by scaffold proteins in mammals
Deborah K Morrison1, Roger J Davis
1Regulation of Cell Growth Laboratory, NCI-Frederick, P.O. Box B, Frederick, Maryland 21702, USA. dmorrison@ncifcrf.gov
Abstract:
The 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.
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