Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation.
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Brondello JM, Pouyssegur J, McKenzie FR
Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation.
Science. 1999 Dec 24;286(5449):2514-7.
- PubMed ID
- 10617468 [ View in PubMed]
- 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 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.