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MKP5 is a member of DS-MKP family.[1] It is a dual-specificity phosphoprotein phosphatase. This means that MKP5 dephosophorylates and in turn deactivates a few different MAPK. Its structural features include the presence of an N-terminus (NT) domain of unknown function in addition to the MKB and DSP domains that are characteristic of other members of DS-MKP family. MKP5 shows preference for dephosphorylating JNK and p38 MAPKs but not ERK. It has been hypothesized that the novel NT domain is possibly a protein interaction domain that may be involved in interaction with other cellular proteins and thereby providing a mechanism for cross-talk between MAPK and other signaling pathways involved in regulating cellular functions. The NT domain thus suggests another element of complexity in the biological function of DS-MKPs.
References
[edit]- ^ Theodosiou A, Smith A, Gillieron C, Arkinstall S, Ashworth A (November 1999). "MKP5, a new member of the MAP kinase phosphatase family, which selectively dephosphorylates stress-activated kinases". Oncogene. 18 (50): 6981–8. doi:10.1038/sj.onc.1203185. PMID 10597297.