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Reduced MAP Kinase Phosphatase-1 Degradation After p42/p44MAPK-Dependent Phosphorylation

Science  24 Dec 1999:
Vol. 286, Issue 5449, pp. 2514-2517
DOI: 10.1126/science.286.5449.2514

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Abstract

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 p42MAPK or p44MAPK, 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 p44MAPK but led to stabilization of the protein. These results illustrate the importance of regulated protein degradation in the control of mitogenic signaling.

  • * Present address: The Scripps Research Institute, Department of Molecular Biology, MB-3, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

  • To whom correspondence should be addressed. E-mail: mckenzie{at}unice.fr

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