Isolation and characterization of a Drosophila homologue of mitogen-activated protein kinase phosphatase-3 which has a high substrate specificity towards extracellular-signal-regulated kinase.
作者： Sun-Hong KIM , Hyung-Bae KWON , Yong-Sik KIM , Ji-Hwan RYU , Kyung-Sub KIM
DOI: 10.1042/BJ3610143
关键词:
摘要: A partial C-terminal cDNA sequence of a novel Drosophila mitogen-activated protein kinase phosphatase (MKP), designated DMKP-3, was identified from an epitope expressed tag database, and the missing N-terminal fragment cloned library. DMKP-3 is 411 amino acids, with calculated molecular mass 45.8 kDa; deduced acid most similar to that mammalian MKP-3. Recombinant produced in Escherichia coli retained intrinsic tyrosine activity. In addition, specifically inhibited extracellular-signal-regulated (ERK) activity, but without significant affect on c-Jun (JNK) p38 activities, when it overexpressed Schneider cells. interacted ERK (DERK) via its domain. Elk-1-dependent trans-reporter gene expression CV1 cells, dephosphorylated activated vitro. uniquely localized cytoplasm within tightly regulated during development. Thus homologue MKP-3, may play important roles regulation various developmental processes.
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