Key result
More than one calmodulin molecule can bind to the CaV1.2 C-terminal tail at high calcium concentrations, with the C-lobe being critical for sensing calcium changes.
Why the study?
The binding modes and concentration- and Ca2+-dependencies of calmodulin interactions with the C- and N-terminal tails of the CaV1.2 channel were not fully characterized.
Answers are grounded in this paper and cite their sources.
This basic science study elucidates the specific Ca2+-dependent binding mechanics between calmodulin and the CaV1.2 channel, highlighting the critical role of the CaM C-lobe.
This study examined the bindings of calmodulin (CaM) and its mutants with the C- and N-terminal tails of the voltage-gated Ca(2+) channel CaV1.2 at different CaM and Ca(2+) concentrations ([Ca(2+)]) by using the pull-down assay method to obtain basic information on the binding mode, including its concentration- and Ca(2+)-dependencies. Our data show that more than one CaM molecule could bind to the CaV1.2 C-terminal tail at high [Ca(2+)]. Additionally, the C-lobe of CaM is highly critical in sensing the change of [Ca(2+)] in its binding to the C-terminal tail of CaV1.2, and the binding between CaM and the N-terminal tail of CaV1.2 requires high [Ca(2+)]. Our data provide new details on the interactions between CaM and the CaV1.2 channel.
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He et al. (2013) studied this question. Calmodulin (CaM) and its mutants vs. Ca2+-free condition was evaluated on Binding of CaM to CaV1.2 C- and N-terminal tails. More than one calmodulin molecule can bind to the CaV1.2 C-terminal tail at high calcium concentrations, with the C-lobe being critical for sensing calcium changes.
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