PMID- 10753652
OWN - NLM
STAT- MEDLINE
DCOM- 20000508
LR  - 20131121
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 270
IP  - 2
DP  - 2000 Apr 13
TI  - Skeletal muscle CaMKII enriches in nuclei and phosphorylates myogenic factor SRF 
      at multiple sites.
PG  - 488-94
AB  - We characterized the activity of Ca(2+)/calmodulin-dependent protein kinase II 
      (CaMKII) in homogenates and nuclear extracts of skeletal muscle and analyzed 
      their capacity to phosphorylate the myogenic factor SRF. Isoforms of CaMKII 
      enriched from skeletal muscle phosphorylated SRF in vitro to high stoichiometries 
      and produced multiple forms on SDS-PAGE, suggesting that SRF was phosphorylated 
      at multiple sites. Phosphopeptide-mapping experiments using truncated SRF 
      proteins located the residues of SRF phosphorylated by recombinant CaMKII within 
      amino acids 1-171, with at least one site residing in amino acids 142-171. 
      Microsequencing of these phosphorylated peptides identified that both Ser-103 and 
      a novel residue, Thr-160 in the MADS box of SRF, were sites of phosphorylation. 
      CaMKII activity was enriched in nuclear extracts relative to crude homogenates 
      from skeletal muscle and similarly phosphorylated the nuclear transcription 
      factor SRF in vitro. The location of Thr-160 in the 3-D structure of SRF suggests 
      that its phosphorylation by nuclear CaMKII may directly influence DNA binding of 
      SRF and other MADS box factors.
CI  - Copyright 2000 Academic Press.
FAU - Fluck, M
AU  - Fluck M
AD  - Department of Integrative Biology and Pharmacology, University of Texas Medical 
      School, Houston, Texas 77030, USA. flueck@mem.unibe.ch
FAU - Booth, F W
AU  - Booth FW
FAU - Waxham, M N
AU  - Waxham MN
LA  - eng
GR  - AR19393/AR/NIAMS NIH HHS/United States
GR  - NS26086/NS/NINDS 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  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Serum Response Factor)
RN  - 2ZD004190S (Threonine)
RN  - 452VLY9402 (Serine)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Type 2)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Calcium-Calmodulin-Dependent Protein Kinase Type 2
MH  - Calcium-Calmodulin-Dependent Protein Kinases/*metabolism
MH  - Cell Nucleus/*enzymology
MH  - Chickens
MH  - DNA-Binding Proteins/chemistry/*metabolism
MH  - Molecular Sequence Data
MH  - Muscle, Skeletal/*enzymology
MH  - Nuclear Proteins/chemistry/*metabolism
MH  - Peptide Mapping
MH  - Phosphorylation
MH  - Rats
MH  - Serine/metabolism
MH  - Serum Response Factor
MH  - Threonine/metabolism
OTO - NASA
OT  - Non-programmatic
EDAT- 2001/02/07 11:00
MHDA- 2001/02/07 11:01
CRDT- 2001/02/07 11:00
PHST- 2001/02/07 11:00 [pubmed]
PHST- 2001/02/07 11:01 [medline]
PHST- 2001/02/07 11:00 [entrez]
AID - S0006-291X(00)92457-4 [pii]
AID - 10.1006/bbrc.2000.2457 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2000 Apr 13;270(2):488-94. doi: 
      10.1006/bbrc.2000.2457.