CaMKII phosphorylates a threonine residue in the C-terminal tail of Cav1.2 Ca2+ channel and modulates the interaction of the channel with calmodulin

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Structured PICO

Population

Guinea-pig Cav1.2 Ca(2+) channel model

Intervention

Mutation of Thr1603 to Asp (T1603D) and CaMKII-mediated phosphorylation

Comparator

Wild-type channel / unphosphorylated state

Outcome

Channel run-down in inside-out patch mode and calmodulin (CaM) binding to the proximal C-terminal fragment (CT1)surrogate

CaMKII phosphorylates the Thr1603 residue on the Cav1.2 channel, which regulates calmodulin binding and maintains the channel's basal activity.

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Thr1603 phosphorylation may stabilize Cav1.2 activity; leaves open its relevance to human cardiac excitability and need for in vivo validation.

Wang et al. (2009) studied this question.

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Thr1603 phosphorylation may stabilize Cav1.2 activity; leaves open its relevance to human cardiac excitability and need for in vivo validation.