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

Science (New York, N.Y.) | Dec 24, 1999

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 RIS Download

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

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Associated grants

  • Agency: NIGMS NIH HHS, Id: GM26939

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