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 kinase that lie upstream of yeast MAP kinase homologues in the pheromone-dependent mating pathways.
Original language | English |
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Pages (from-to) | 183-189 |
Number of pages | 7 |
Journal | FEBS Letters |
Volume | 308 |
Issue number | 2 |
DOIs | |
Publication status | Published - 17 Aug 1992 |
Keywords
- Mitogen-activated protein (MAP) kinase
- Pheromone
- Protein kinase
- Signal transduction
- Yeast
ASJC Scopus subject areas
- Structural Biology
- Biophysics
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology