作者: Marijane Russell , Carol A. Lange-Carter , Gary L. Johnson
DOI: 10.1021/BI00020A005
关键词:
摘要: Mitogen-activated protein kinase (MAPK) activation is an important signal involved in regulating cellular proliferation and/or differentiation. The immediate upstream MAPK kinase, referred to as MEK, activates by phosphorylation on specific tyrosine and threonine residues. To date, two MEK's have been cloned characterized, MEK1 MEK2. Here we report the cloning of MEK2b from mouse pituitary cDNA. Rat MEK2 amino acid sequences vary only three acids; changes are conserved sequence. Analysis recombinant demonstrated similar kinases phosphotransferase activity toward MAPK, while they differed autophosphorylation ability serve a substrate for MAPK. findings demonstrate significant differences potential regulatory mechanisms MEK2/2b but not their regulators.