A Novel MAPK Phosphatase MKP-7 Acts Preferentially on JNK/SAPK and p38α and β MAPKs*
By T. Tanoue, Takuya Yamamoto, R. Maeda, E. Nishida. Journal of Biological Chemistry, 2001
155 citations recorded by the source corpus.
Mitogen-activated protein kinases (MAPKs) are inactivated via dephosphorylation of either the threonine or tyrosine residue or both in the P-loop catalyzed by protein phosphatases which include serine/threonine phosphatases, tyrosine phosphatases, and dual specificity phosphatases. Nine members of the dual specificity phosphatases specific for MAPKs, termed MKPs, have been reported. Each member has its own substrate specificity, tissue distribution, and subcellular localization. In this study, we have cloned and characterized a novel MKP, designated MKP-7. MKP-7 is most similar to hVH5, a member of previously known MKPs, in the primary structure. MKP-7 is predominantly localized in the cytoplasm when expressed in cultured cells, whereas hVH5 is both in the nucleus and the cytoplasm. MKP-7 binds to and inactivates p38 MAPK and JNK/SAPK, but not ERK. Furthermore, we have found that MKPs have the substrate specificity toward the isoforms of the p38 family (α, β, γ, and δ). MKP-7 binds to and inactivates p38α and -β, but not γ or δ. MKP-5 and CL100/MKP-1 also bind to p38α and -β, but not γ or δ. Finally, we propose a tentative classification of MKPs based on the sequence characteristics of their MAPK-docking site.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/e99aecb3e71859c9a92003d296d7e85482d180d6
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Citations in the corpus
- Differential regulation of MAP kinase signalling by dual-specificity protein phosphatases (2007, background): “It was subsequently demonstrated that other MKPs such as DUSP8, DUSP10/MKP-5 and DUSP16/MKP-7 are able to selectively inactivate JNK and p38 but not ERK1/2 whereas others such as DUSP1/MKP-1 can regulate all three classes of MAPK (Muda et al., 1996; Tanoue et al., 1999, 2001b; Slack et al., 2001).”