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Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation.

The mitogen-activated protein (MAP) kinase cascade is inactivated at the level of MAP kinase by members of the MAP kinase phosphatase (MKP) family, including MKP-1. MKP-1 was a labile protein in CCL39 hamster fibroblasts; its degradation was attenuated by inhibitors of the ubiquitin-directed proteasome complex. MKP-1 was a target in vivo and in vitro for p42(MAPK) or p44(MAPK), which phosphorylates MKP-1 on two carboxyl-terminal serine residues, Serine 359 and Serine 364. This phosphorylation did not modify MKP-1's intrinsic ability to dephosphorylate p44(MAPK) but led to stabilization of the protein. These results illustrate the importance of regulated protein degradation in the control of mitogenic signaling.

Pubmed ID: 10617468

Authors

  • Brondello JM
  • Pouyss√©gur J
  • McKenzie FR

Journal

Science (New York, N.Y.)

Publication Data

December 24, 1999

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM26939

Mesh Terms

  • Animals
  • Blood
  • Cell Cycle Proteins
  • Cell Division
  • Cell Line
  • Cricetinae
  • Culture Media
  • Cysteine Endopeptidases
  • Cysteine Proteinase Inhibitors
  • Dual Specificity Phosphatase 1
  • Estradiol
  • Humans
  • Immediate-Early Proteins
  • Leucine
  • Leupeptins
  • MAP Kinase Signaling System
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases
  • Multienzyme Complexes
  • Mutation
  • Nitrophenols
  • Organophosphorus Compounds
  • Phosphoprotein Phosphatases
  • Phosphorylation
  • Proteasome Endopeptidase Complex
  • Protein Phosphatase 1
  • Protein Tyrosine Phosphatases
  • Ubiquitins