Single-Channel Resolution of the Interaction between C-Terminal Ca_V1.3 Isoforms and Calmodulin.

ABSTRACT: Voltage-dependent calcium (Ca_V) 1.3 channels are involved in the control of cellular excitability and pacemaking in neuronal, cardiac, and sensory cells. Various proteins interact with the alternatively spliced channel C-terminus regulating gating of Ca_V1.3 channels. Binding of a regulatory calcium-binding protein calmodulin (CaM) to the proximal C-terminus leads to the boosting of channel activity and promotes calcium-dependent inactivation (CDI). The C-terminal modulator domain (CTM) of Ca_V1.3 channels can interfere with the CaM binding, thereby inhibiting channel activity and CDI. Here, we compared single-channel gating behavior of two natural Ca_V1.3 splice isoforms: the long Ca_V1.3₄₂ with the full-length CTM and the shor

SUBMITTER: Kuzmenkina E 

PROVIDER: S-EPMC6403076 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature