Identification of MAP kinase domains by redirecting stress signals into growth factor responses

Science. 1996 Jun 14;272(5268):1652-5. doi: 10.1126/science.272.5268.1652.

Abstract

Mitogen-activated protein kinase (MAPK) cascades, termed MAPK modules, channel extracellular signals into specific cellular responses. Chimeric molecules were constructed between p38 and p44 MAPKs, which transduce stress and growth factor signals, respectively. A discrete region of 40 residues located in the amono-terminal p38MAPK lobe directed the specificity of response to extracellular signals, whereas the p44MAPK chimera, expressed in vivo, redirected stress signals into early mitogenic responses, demonstrating the functional independence of these domains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anisomycin / pharmacology
  • Binding Sites
  • Calcium-Calmodulin-Dependent Protein Kinases / genetics
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Cell Division
  • Cell Line
  • Cricetinae
  • Cricetulus
  • Enzyme Activation
  • Gene Expression Regulation
  • Genes, fos
  • Growth Substances / metabolism
  • Mice
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases*
  • Molecular Sequence Data
  • Phosphorylation / drug effects
  • Protein Kinases / metabolism
  • Protein Serine-Threonine Kinases / metabolism
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Ribosomal Protein S6 Kinases
  • Signal Transduction
  • Sorbitol / pharmacology
  • Substrate Specificity
  • p38 Mitogen-Activated Protein Kinases

Substances

  • Growth Substances
  • Recombinant Fusion Proteins
  • Sorbitol
  • Anisomycin
  • Protein Kinases
  • Protein Serine-Threonine Kinases
  • Ribosomal Protein S6 Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases