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Regulation of map kinase signaling modules by scaffold proteins in mammals

  1. Author:
    Morrison, D. K.
    Davis, R. J.

  2. Author Address

    NCI, Regulat Cell Growth Lab, POB B, Frederick, MD 21702 USA NCI, Regulat Cell Growth Lab, Frederick, MD 21702 USA Univ Massachusetts, Sch Med, Howard Hughes Med Inst, Worcester, MA 01605 USA Univ Massachusetts, Sch Med, Program Mol Med, Worcester, MA 01605 USA Morrison DK NCI, Regulat Cell Growth Lab, POB B, Frederick, MD 21702 USA
    1. Year: 2003
  2. Journal: Annual Review of Cell and Developmental Biology
    1. 19
    2. Pages: 91-118
  4. Type of Article: Article
  1. 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 (INK), 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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