PMID- 10637505
OWN - NLM
STAT- MEDLINE
DCOM- 20000204
LR  - 20091119
IS  - 0950-9232 (Print)
IS  - 0950-9232 (Linking)
VI  - 18
IP  - 56
DP  - 1999 Dec 23
TI  - ERK activation induces phosphorylation of Elk-1 at multiple S/T-P motifs to high 
      stoichiometry.
PG  - 7948-57
AB  - Elk-1, a member of the TCF family of Ets domain proteins, contains a C-terminal
      transcriptional activation domain with multiple copies of the MAPK core consensus
      sequence S/T-P. This region is phosphorylated by MAP kinases in vitro and in
      vivo, but the extent and kinetics of phosphorylation at the different sites have 
      not been investigated in detail. We prepared antisera against the phosphorylated 
      forms of residues T353, T363, T368, S383, S389 and T417. The antisera
      specifically recognize the phosphorylated Elk-1 C terminus and are specific for
      their cognate sites, as assessed by peptide competition and mutagenesis
      experiments. Analysis of cells stably expressing Elk-1 in vivo shows that
      following serum or TPA stimulation, residues T353, T363, T368, S383, S389 and
      T417 become phosphorylated with similar kinetics. Mutation of any one site does
      not prevent phosphorylation of the others. Mutation to alanine of S383, F378 or
      W379, which virtually abolishes transcriptional activation by Elk-1, does not
      affect phosphorylation of any sites tested. Analysis of Elk-1 using
      two-dimensional gel electrophoresis shows that following ERK activation Elk-1
      receives at least six phosphates in addition to those present prior to
      stimulation. We propose that the Elk-1 C-terminal regulatory domain becomes
      stoichiometrically phosphorylated following growth factor stimulation.
FAU - Cruzalegui, F H
AU  - Cruzalegui FH
AD  - Transcription Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields,
      London WC2A 3PX, UK.
FAU - Cano, E
AU  - Cano E
FAU - Treisman, R
AU  - Treisman R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Oncogene
JT  - Oncogene
JID - 8711562
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (ELK1 protein, human)
RN  - 0 (Elk1 protein, mouse)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Transcription Factors)
RN  - 0 (ets-Domain Protein Elk-1)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
SB  - IM
MH  - 3T3 Cells
MH  - Amino Acid Sequence
MH  - Amino Acid Substitution
MH  - Animals
MH  - *DNA-Binding Proteins
MH  - Enzyme Activation
MH  - Humans
MH  - Kinetics
MH  - Mice
MH  - Mitogen-Activated Protein Kinases/*metabolism
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Phosphorylation
MH  - Point Mutation
MH  - Proto-Oncogene Proteins/chemistry/genetics/*metabolism
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Transcription Factors/chemistry/metabolism
MH  - Transcription, Genetic
MH  - Transfection
MH  - ets-Domain Protein Elk-1
EDAT- 2000/01/19 00:00
MHDA- 2000/01/19 00:01
CRDT- 2000/01/19 00:00
PHST- 2000/01/19 00:00 [pubmed]
PHST- 2000/01/19 00:01 [medline]
PHST- 2000/01/19 00:00 [entrez]
AID - 10.1038/sj.onc.1203362 [doi]
PST - ppublish
SO  - Oncogene. 1999 Dec 23;18(56):7948-57. doi: 10.1038/sj.onc.1203362.