dual specificity protein phosphatase 1, MAP kinase phosphatase 1 or CL100 phosphatase
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Function
- dual specificity tyrosine/serine-threonine phosphatase
- highly specific for MAP kinases
- dephosphorylates MAP kinase ERK2 on both Thr-183 & Tyr-185
- inhibits DNA synthesis induced by constitutively active p21ras[3]
protein tyrosine phosphate + H2O
<-->
protein tyrosine + phosphate
phosphoprotein + H2O <--> a protein + phosphate
Structure
- belongs to the protein-tyrosine phosphatase family
- non-receptor class dual specificity subfamily
- contains 1 rhodanese domain
- contains 1 tyrosine-protein phosphatase domain
Expression
- expressed at high levels in the lung, liver placenta & pancreas
- moderate levels seen in the heart & skeletal muscle
- lower levels found in the brain & kidney
- induced by oxidative stress & heat shock
- isolated from fibroblasts exposed to oxidative stress or heat shock
- induced by mitogenic stimulation ?
More general terms
References
- ↑ Sun H, Charles CH, Lau LF, Tonks NK. MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell. 1993 Nov 5;75(3):487-93. PMID: https://www.ncbi.nlm.nih.gov/pubmed/8221888
- ↑ Nebreda AR. Inactivation of MAP kinases. Trends Biochem Sci. 1994 Jan;19(1):1-2. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/8140614
- ↑ 3.0 3.1 Sun H, Tonks NK, Bar-Sagi D. Inhibition of Ras-induced DNA synthesis by expression of the phosphatase MKP-1. Science. 1994 Oct 14;266(5183):285-8. PMID: https://www.ncbi.nlm.nih.gov/pubmed/7939666
- ↑ UniProt http://www.uniprot.org/uniprot/P28562.html