Translocatable voltage-gated Ca²⁺ channel β subunits in α1-β complexes reveal competitive replacement yet no spontaneous dissociation.

ABSTRACT: β subunits of high voltage-gated Ca²⁺ (Ca_V) channels promote cell-surface expression of pore-forming α1 subunits and regulate channel gating through binding to the α-interaction domain (AID) in the first intracellular loop. We addressed the stability of Ca_V α1B-β interactions by rapamycin-translocatable Ca_V β subunits that allow drug-induced sequestration and uncoupling of the β subunit from Ca_V2.2 channel complexes in intact cells. Without Ca_V α1B/α2δ1, all modified β subunits, except membrane-tethered β2a and β2e, are in the cytosol and rapidly translocate upon rapamycin addition to anchors on target organelles: plasma membrane, mitochondria, or endoplasmic reticulum. In cells coexpressing Ca_V α1B/α2δ1 subunits,

SUBMITTER: Yeon JH 

PROVIDER: S-EPMC6196550 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature