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

Article Details

Citation

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Mitogen-activated protein kinase 1P28482Details
Mitogen-activated protein kinase 3P27361Details