PMID- 10567369
OWN - NLM
STAT- MEDLINE
DCOM- 19991229
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 48
DP  - 1999 Nov 26
TI  - The N-terminal ERK-binding site of MEK1 is required for efficient feedback
      phosphorylation by ERK2 in vitro and ERK activation in vivo.
PG  - 34029-35
AB  - An ERK2-binding site at the N terminus of MEK1 was reported to mediate their
      stable association. We examined the importance of this binding site in the
      feedback phosphorylation of MEK1 on Thr(292) and Thr(386) by ERK2, the
      phosphorylation and activation of ERK2 by MEK1, and the interaction of MEK1 with 
      ERK2 and Raf-1. Deletion of the binding site from MEK1 reduced its
      phosphorylation by ERK2, but had no effect on its phosphorylation by
      p21-activated protein kinase-1 (PAK1). A MEK1 N-terminal peptide containing the
      binding site inhibited MEK1 phosphorylation by ERK2. However, it did not affect
      MEK1 phosphorylation by p21-activated protein kinase or myelin basic protein
      phosphorylation by ERK2. Deletion of the N-terminal ERK-binding domain of MEK1
      also reduced its ability to phosphorylate ERK2 in vitro, to co-immunoprecipitate 
      with ERK2, and to stimulate ERK2 activation in transfected cells, but it did not 
      alter the association with endogenous Raf-1. Using ERK2-p38 chimeras and an ERK2 
      deletion mutant, a MEK1-binding site of ERK2 was localized to its N terminus.
FAU - Xu, B e
AU  - Xu Be
AD  - Department of Pharmacology, University of Texas Southwestern Medical Center,
      Dallas, Texas 75235-9041, USA.
FAU - Wilsbacher, J L
AU  - Wilsbacher JL
FAU - Collisson, T
AU  - Collisson T
FAU - Cobb, M H
AU  - Cobb MH
LA  - eng
GR  - DK34128/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Oligopeptides)
RN  - 2ZD004190S (Threonine)
RN  - EC 2.7.11.1 (PAK1 protein, human)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (Proto-Oncogene Proteins c-raf)
RN  - EC 2.7.11.1 (p21-Activated Kinases)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
RN  - EC 2.7.12.2 (MAP Kinase Kinase 1)
RN  - EC 2.7.12.2 (MAP2K1 protein, human)
RN  - EC 2.7.12.2 (Mitogen-Activated Protein Kinase Kinases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites/genetics
MH  - Binding, Competitive
MH  - Cell Line
MH  - Enzyme Activation
MH  - Humans
MH  - MAP Kinase Kinase 1
MH  - Mitogen-Activated Protein Kinase 1/*metabolism
MH  - Mitogen-Activated Protein Kinase Kinases/chemistry/genetics/*metabolism
MH  - Mitogen-Activated Protein Kinases/*metabolism
MH  - Molecular Sequence Data
MH  - Oligopeptides/chemical synthesis/metabolism
MH  - Phosphorylation
MH  - Protein Binding
MH  - Protein-Serine-Threonine Kinases/metabolism
MH  - Proto-Oncogene Proteins c-raf/metabolism
MH  - Sequence Deletion
MH  - Threonine/metabolism
MH  - Time Factors
MH  - p21-Activated Kinases
EDAT- 1999/11/24 00:00
MHDA- 1999/11/24 00:01
CRDT- 1999/11/24 00:00
PHST- 1999/11/24 00:00 [pubmed]
PHST- 1999/11/24 00:01 [medline]
PHST- 1999/11/24 00:00 [entrez]
AID - 10.1074/jbc.274.48.34029 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Nov 26;274(48):34029-35. doi: 10.1074/jbc.274.48.34029.