Hydrophobic as Well as Charged Residues in Both MEK1 and ERK2 Are Important for Their Proper Docking
Open Access
- 1 July 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (28) , 26509-26515
- https://doi.org/10.1074/jbc.m102769200
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological FunctionsEndocrine Reviews, 2001
- Creation of a Stress-activated p90 Ribosomal S6 KinaseJournal of Biological Chemistry, 2000
- WNK1, a Novel Mammalian Serine/Threonine Protein Kinase Lacking the Catalytic Lysine in Subdomain IIJournal of Biological Chemistry, 2000
- A conserved docking motif in MAP kinases common to substrates, activators and regulatorsNature Cell Biology, 2000
- The N-terminal ERK-binding Site of MEK1 Is Required for Efficient Feedback Phosphorylation by ERK2 in Vitro and ERK Activation in VivoJournal of Biological Chemistry, 1999
- MEKK1 interacts with ?-actinin and localizes to stress fibers and focal adhesionsCell Motility, 1999
- Phosphorylation of MAP Kinases by MAP/ERK Involves Multiple Regions of MAP KinasesPublished by Elsevier ,1999
- The MEK1 Proline-rich Insert Is Required for Efficient Activation of the Mitogen-activated Protein Kinases ERK1 and ERK2 in Mammalian CellsPublished by Elsevier ,1998
- Deuterium Exchange Mass Spectrometry as a Probe of Protein Kinase Activation. Analysis of Wild-Type and Constitutively Active Mutants of MAP Kinase Kinase-1Biochemistry, 1998
- Identification of MAP Kinase Domains by Redirecting Stress Signals into Growth Factor ResponsesScience, 1996