Regulation of phosphorylation at the postsynaptic density during different activity states of Ca2+/calmodulin-dependent protein kinase II.

ABSTRACT: 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 desc

SUBMITTER: Dosemeci A 

PROVIDER: S-EPMC2812614 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature