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Significance Calmodulin (CaM) regulation of voltage-gated calcium (CaV ) channels constitutes a prototypic biological feedback mechanism that contributes prominently toward Ca2+ homeostasis in neurons and cardiac myocytes. Here, by partitioning CaM molecularly into its two elemental domains or lobes, we uncover a distinctive nonlinearity in CaM signaling to CaV channels. CaV channels detect the coincident binding of two CaM lobes to up-regulate channel activity. This mechanism elaborates a molecular logic operation that enables channels to detect combinations of spatiotemporal Ca2+ signals and perform higher-order computations on Ca2+ signals. These findings uncover the unified mechanistic basis for CaV channel feedback and, in so doing, shed light on the versatility of CaM in decoding cellular Ca2+ signals.

Bilobal architecture is a requirement for calmodulin signaling to Ca V 1.3 channels

Bilobal architecture is a requirement for calmodulin signaling to Ca _V 1.3 channels