PMID- 10617468 OWN - NLM STAT- MEDLINE DCOM- 20000111 LR - 20190619 IS - 0036-8075 (Print) IS - 0036-8075 (Linking) VI - 286 IP - 5449 DP - 1999 Dec 24 TI - Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation. PG - 2514-7 AB - 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. FAU - Brondello, J M AU - Brondello JM AD - Institute of Signaling, Developmental Biology and Cancer Research, CNRS UMR 6543, Centre A. Lacassagne, 33 Avenue de Valombrose, Nice 06189, France. FAU - Pouyssegur, J AU - Pouyssegur J FAU - McKenzie, F R AU - McKenzie FR LA - eng GR - GM26939/GM/NIGMS NIH HHS/United States PT - Journal Article PT - Research Support, Non-U.S. Gov't PT - Research Support, U.S. Gov't, P.H.S. PL - United States TA - Science JT - Science (New York, N.Y.) JID - 0404511 RN - 0 (Cell Cycle Proteins) RN - 0 (Culture Media) RN - 0 (Cysteine Proteinase Inhibitors) RN - 0 (Immediate-Early Proteins) RN - 0 (Leupeptins) RN - 0 (Multienzyme Complexes) RN - 0 (Nitrophenols) RN - 0 (Organophosphorus Compounds) RN - 0 (Ubiquitins) RN - 110044-82-1 (acetylleucyl-leucyl-norleucinal) RN - 330-13-2 (nitrophenylphosphate) RN - 4TI98Z838E (Estradiol) RN - EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1) RN - EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3) RN - EC 2.7.11.24 (Mitogen-Activated Protein Kinases) RN - EC 3.1.3.16 (Phosphoprotein Phosphatases) RN - EC 3.1.3.16 (Protein Phosphatase 1) RN - EC 3.1.3.48 (DUSP1 protein, human) RN - EC 3.1.3.48 (Dual Specificity Phosphatase 1) RN - EC 3.1.3.48 (Protein Tyrosine Phosphatases) RN - EC 3.4.22.- (Cysteine Endopeptidases) RN - EC 3.4.25.1 (Proteasome Endopeptidase Complex) RN - GMW67QNF9C (Leucine) RN - R76F7856MV (E 64) SB - IM MH - Animals MH - Blood MH - *Cell Cycle Proteins MH - Cell Division MH - Cell Line MH - Cricetinae MH - Culture Media MH - Cysteine Endopeptidases/metabolism MH - Cysteine Proteinase Inhibitors/pharmacology MH - Dual Specificity Phosphatase 1 MH - Estradiol/pharmacology MH - Humans MH - Immediate-Early Proteins/chemistry/*metabolism MH - Leucine/analogs & derivatives/pharmacology MH - Leupeptins/pharmacology MH - MAP Kinase Signaling System MH - Mitogen-Activated Protein Kinase 1/*metabolism MH - Mitogen-Activated Protein Kinase 3 MH - Mitogen-Activated Protein Kinases/*metabolism MH - Multienzyme Complexes/metabolism MH - Mutation MH - Nitrophenols/metabolism MH - Organophosphorus Compounds/metabolism MH - *Phosphoprotein Phosphatases MH - Phosphorylation MH - Proteasome Endopeptidase Complex MH - Protein Phosphatase 1 MH - Protein Tyrosine Phosphatases/chemistry/*metabolism MH - Ubiquitins/metabolism EDAT- 2000/01/05 00:00 MHDA- 2000/01/05 00:01 CRDT- 2000/01/05 00:00 PHST- 2000/01/05 00:00 [pubmed] PHST- 2000/01/05 00:01 [medline] PHST- 2000/01/05 00:00 [entrez] AID - 8131 [pii] AID - 10.1126/science.286.5449.2514 [doi] PST - ppublish SO - Science. 1999 Dec 24;286(5449):2514-7. doi: 10.1126/science.286.5449.2514.