PMID- 19896464
OWN - NLM
STAT- MEDLINE
DCOM- 20100315
LR  - 20220321
IS  - 1090-2104 (Electronic)
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 391
IP  - 1
DP  - 2010 Jan 1
TI  - Regulation of phosphorylation at the postsynaptic density during different 
      activity states of Ca2+/calmodulin-dependent protein kinase II.
PG  - 78-84
LID - 10.1016/j.bbrc.2009.10.167 [doi]
AB  - Ca(2+)/calmodulin-dependent protein kinase II (CaMKII), the most abundant kinase 
      at the postsynaptic density (PSD), is expected to be involved in activity-induced 
      regulation of synaptic properties. CaMKII is activated when it binds calmodulin 
      in the presence of Ca(2+) and, once autophosphorylated on T-286/7, remains active 
      in the absence of Ca(2+) (autonomous form). In the present study we used a 
      quantitative mass spectrometric strategy (iTRAQ) to identify sites on PSD 
      components phosphorylated upon CaMKII activation. Phosphorylation in isolated 
      PSDs was monitored under conditions where CaMKII is: (1) mostly inactive (basal 
      state), (2) active in the presence of Ca(2+), and (3) active in the absence of 
      Ca(2+). The quantification strategy was validated through confirmation of 
      previously described autophosphorylation characteristics of CaMKII. The 
      effectiveness of phosphorylation of major PSD components by the activated CaMKII 
      in the presence and absence of Ca(2+) varied. Most notably, autonomous activity 
      in the absence of Ca(2+) was more effective in the phosphorylation of three 
      residues on SynGAP. Several PSD scaffold proteins were phosphorylated upon 
      activation of CaMKII. The strategy adopted allowed the identification, for the 
      first time, of CaMKII-regulated sites on SAPAPs and Shanks, including three 
      conserved serine residues near the C-termini of SAPAP1, SAPAP2, and SAPAP3. 
      Involvement of CaMKII in the phosphorylation of PSD scaffold proteins suggests a 
      role in activity-induced structural re-organization of the PSD.
CI  - Published by Elsevier Inc.
FAU - Dosemeci, Ayse
AU  - Dosemeci A
AD  - Laboratory of Neurobiology, NINDS, NIH, Bethesda, MD 20892, USA. 
      dosemeca@mail.nih.gov
FAU - Jaffe, Howard
AU  - Jaffe H
LA  - eng
GR  - Z99 NS999999/ImNIH/Intramural NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Intramural
DEP - 20091105
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Calmodulin)
RN  - 0 (Dlgap1 protein, rat)
RN  - 0 (Dlgap2 protein, rat)
RN  - 0 (Dlgap3 protein, rat)
RN  - 0 (Nerve Tissue Proteins)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Type 2)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Calcium/metabolism
MH  - Calcium-Calmodulin-Dependent Protein Kinase Type 2/*metabolism
MH  - Calmodulin/metabolism
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/*metabolism
MH  - Phosphorylation
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Synapses/*enzymology
PMC - PMC2812614
MID - NIHMS161645
EDAT- 2009/11/10 06:00
MHDA- 2010/03/17 06:00
PMCR- 2011/01/01
CRDT- 2009/11/10 06:00
PHST- 2009/10/29 00:00 [received]
PHST- 2009/10/31 00:00 [accepted]
PHST- 2009/11/10 06:00 [entrez]
PHST- 2009/11/10 06:00 [pubmed]
PHST- 2010/03/17 06:00 [medline]
PHST- 2011/01/01 00:00 [pmc-release]
AID - S0006-291X(09)02165-2 [pii]
AID - 10.1016/j.bbrc.2009.10.167 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2010 Jan 1;391(1):78-84. doi: 
      10.1016/j.bbrc.2009.10.167. Epub 2009 Nov 5.