| Title: | 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 S; Campbell DG; Cohen P; |
| Address: | "Department of Biochemistry, University of Dundee, Scotland, UK" |
| DOI: | 10.1016/0014-5793(92)81271-m |
| ISSN/ISBN: | 0014-5793 (Print) 0014-5793 (Linking) |
| Abstract: | "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 kinases that lie upstream of yeast MAP kinase homologues in the pheromone-dependent mating pathways" |
| Keywords: | "Amino Acid Sequence Animals Chromatography, Liquid Electrophoresis, Polyacrylamide Gel Mice Mitogen-Activated Protein Kinase Kinases Molecular Sequence Data Muscles/*enzymology Peptide Mapping Pheromones/*metabolism Protein Kinases/genetics/isolation & pu;" |
| Notes: | "MedlineNakielny, S Campbell, D G Cohen, P eng Research Support, Non-U.S. Gov't England 1992/08/17 FEBS Lett. 1992 Aug 17; 308(2):183-9. doi: 10.1016/0014-5793(92)81271-m" |
