Molecular structure of a protein-tyrosine/threonine kinase activating p42 mitogen-activated protein (MAP) kinase: MAP kinase kinase.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Wu, J; Harrison, JK; Vincent, LA; Haystead, C; Haystead, TA; Michel, H; Hunt, DF; Lynch, KR; Sturgill, TW

Published Date

  • January 1, 1993

Published In

Volume / Issue

  • 90 / 1

Start / End Page

  • 173 - 177

PubMed ID

  • 8380494

Pubmed Central ID

  • PMC45622

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.90.1.173


  • eng

Conference Location

  • United States