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Regulation of MAP kinases by MAP kinase phosphatases.

Authors: Kondoh, K  Nishida, E 
Citation: Kondoh K and Nishida E, Biochim Biophys Acta. 2007 Aug;1773(8):1227-37. Epub 2006 Dec 8.
Pubmed: (View Article at PubMed) PMID:17208316
DOI: Full-text: DOI:10.1016/j.bbamcr.2006.12.002

MAP kinase phosphatases (MKPs) catalyze dephosphorylation of activated MAP kinase (MAPK) molecules and deactivate them. Therefore, MKPs play an important role in determining the magnitude and duration of MAPK activities. MKPs constitute a structurally distinct family of dual-specificity phosphatases. The MKP family members share the sequence homology and the preference for MAPK molecules, but they are different in substrate specificity among MAPK molecules, tissue distribution, subcellular localization and inducibility by extracellular stimuli. Our understanding of their protein structure, substrate recognition mechanisms, and regulatory mechanisms of the enzymatic activity has greatly increased over the past few years. Furthermore, although there are a number of MKPs, that have similar substrate specificities, non-redundant roles of MKPs have begun to be identified. Here we focus on recent findings regarding regulation and function of the MKP family members as physiological regulators of MAPK signaling.


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CRRD Object Information
CRRD ID: 2293881
Created: 2008-06-19
Species: All species
Last Modified: 2008-06-19
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.