Mechanistic Basis for Catalytic Activation of Mitogen-activated Protein Kinase Phosphatase 3 by Extracellular Signal-regulated Kinase
Open Access
- 1 March 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (10) , 6749-6757
- https://doi.org/10.1074/jbc.275.10.6749
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Signal transduction by the c-Jun N-terminal kinase (JNK) — from inflammation to developmentCurrent Opinion in Cell Biology, 1998
- Protein phosphatases and the regulation of MAP kinase activitySeminars in Cell & Developmental Biology, 1998
- Mitogen-activated protein kinase pathwaysCurrent Opinion in Cell Biology, 1997
- Mitogen-activated Protein Kinase Phosphatases Inactivate Stress-activated Protein Kinase Pathways in VivoJournal of Biological Chemistry, 1997
- The Dual Specificity Phosphatases M3/6 and MKP-3 Are Highly Selective for Inactivation of Distinct Mitogen-activated Protein KinasesJournal of Biological Chemistry, 1996
- The Mitogen-activated Protein Kinase Phosphatases PAC1, MKP-1, and MKP-2 Have Unique Substrate Specificities and Reduced Activity in Vivo toward the ERK2 sevenmaker MutationJournal of Biological Chemistry, 1996
- Multiple Dual Specificity Protein Tyrosine Phosphatases Are Expressed and Regulated Differentially in Liver Cell LinesPublished by Elsevier ,1995
- Transcriptional Regulation by Extracellular signals: Mechanisms and SpecificityCell, 1995
- Control of MAP kinase activation by the mitogen-induced threonine/tyrosine phosphatase PAC1Nature, 1994
- MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivoCell, 1993