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MAP kinase kinase from rabbit skeletal muscle A novel dual specificity enzyme showing homology to yeast protein kinases involved in pheromone‐dependent signal transduction
Author(s) -
Nakielny Sara,
Campbell David G.,
Cohen Philip
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81271-m
Subject(s) - map2k7 , mitogen activated protein kinase kinase , map kinase kinase kinase , c raf , cyclin dependent kinase 9 , ask1 , biochemistry , biology , cyclin dependent kinase 2 , mapk14 , protein kinase a , kinase , microbiology and biotechnology
MAP kinase kinase (MAPKK) was purified 30,000‐fold to homogeneity from extracts of rabbit skeletal muscle and shown to be a monomeric protein of apparent molecular mass 44 kDa, MAPKK activated the 42 kDa isoform of MAP kinase by phosphorylation of Thr‐183 and Tyr‐185, and phosphorylated itself slowly on tyrosine, threonine and serine residues, establishing that it is a ‘dual specificity’ protein kinase. Peptide sequences from MAPKK were homologous to other protein serine/threonine kinases, especially to the subfamily that includes yeast protein kinase that lie upstream of yeast MAP kinase homologues in the pheromone‐dependent mating pathways.