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- Title
MKP5, a new member of the MAP kinase phosphatase family, which selectively dephosphorylates stress-activated kinases.
- Authors
Theodosiou, Aspasia; Smith, Anna; Gillieron, Corinne; Arkinstall, Steve; Ashworth, Alan
- Abstract
Dual-specificity protein tyrosine phosphatases are a burgeoning family of enzymes, some of which, the MKPs, are implicated in the regulation of mitogen-activated protein (MAP) kinases. MKPs have been shown to reverse the activation of the MAP kinases by hydrolyzing phosphothreonine and phosphotyrosine residues present in the substrates. Here we describe the characterization of a novel member of the MKP family, MKP5. The MKP5 gene, which maps to human chromosome 1q32, is expressed tissue-specifically as two transcripts of approximately 3.4 and 2.4 kb in human liver and skeletal muscle. When expressed in mammalian cells, MKP5 blocks the enzymatic activation of MAP kinases with the selectivity p38approx. JNK/SAPK>>ERK. Immunoprecipitation of endogenous MAP kinases by the catalytically inactive transfected MKP5 demonstrates that it preferentially binds to the p38 and JNK/SAPK kinases. These findings suggest that the selectivity of this phosphatase may be determined at least in part at the level of substrate binding.
- Subjects
PHOSPHATASES; PROTEINS
- Publication
Oncogene, 1999, Vol 18, Issue 50, p6981
- ISSN
0950-9232
- Publication type
Article
- DOI
10.1038/sj.onc.1203185