Molecular structure of a protein-tyrosine/threonine kinase activating p42 mitogen-activated protein (MAP) kinase: MAP kinase kinase.
MAP kinases p42mapk and p44mapk participate in a protein kinase cascade(s) important for signaling in many cell types and contexts. Both MAP kinases are activated in vitro by MAP kinase kinase, a protein-tyrosine and threonine kinase. A MAP kinase kinase cDNA was isolated from a rat kidney library by using peptide sequence data we obtained from MAP kinase kinase isolated from rabbit skeletal muscle. The deduced sequence, containing 393 amino acids (predicted mass, 43.5 kDa), is most similar to byr1 (Bypass of ras1), a yeast protein kinase functioning in the mating pathway induced by pheromones in Schizosaccharomyces pombe. An unusually large insert is present in MAP kinase kinase between domains IX and X and may contribute to protein-protein interactions with MAP kinase. Major (2.7 kilobases) and minor (1.7 kilobases) transcripts are widely expressed in rat tissues and appear to be derived from a single gene.
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Related Subject Headings
- Sequence Homology, Amino Acid
- Rats
- Rabbits
- RNA, Messenger
- Protein Kinases
- Polymerase Chain Reaction
- Organ Specificity
- Oligodeoxyribonucleotides
- Muscles
- Molecular Sequence Data
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Sequence Homology, Amino Acid
- Rats
- Rabbits
- RNA, Messenger
- Protein Kinases
- Polymerase Chain Reaction
- Organ Specificity
- Oligodeoxyribonucleotides
- Muscles
- Molecular Sequence Data