Key result
Multiple intracellular molecules, including calmodulin, CaBP1, CaMKII, and AKAPs, interact with the CaV1.2 channel and its auxiliary subunits to regulate L-type calcium current kinetics and expression.
This review provides a comprehensive overview of the complex intracellular molecular interactions that regulate the voltage-dependent L-type calcium channel CaV1.2.
Ca(V)1.2 (alpha(1c)) is a pore-forming subunit of the voltage-dependent L-type calcium channel and is expressed in many tissues. The beta and alpha(2)/delta subunits are auxiliary subunits that affect the kinetics and the expression of Ca(V)1.2. In addition to the beta and alpha(2)/delta subunits, several molecules have been reported to be involved in the regulation of Ca(V)1.2 current. Calmodulin, CaBP1 (calcium-binding protein-1), CaMKII (calcium/calmodulin-dependent protein kinase II), AKAPs (A-kinase anchoring proteins), phosphatases, Caveolin-3, beta(2)-adrenergic receptor, PDZ domain proteins, sorcin, SNARE proteins, synaptotagmin, CSN5, RGK family, and AHNAK1 have all been reported to interact with Ca(V)1.2 and the beta subunit. This review focuses on the effect of these molecules on Ca(V)1.2 current.
No takes yet. Share an insight, caveat, or question.
Kobayashi et al. (2007) conducted a review in CaV1.2 channel regulation. Intracellular molecules (e.g., Calmodulin, CaBP1, CaMKII, AKAPs) was evaluated. Multiple intracellular molecules, including calmodulin, CaBP1, CaMKII, and AKAPs, interact with the CaV1.2 channel and its auxiliary subunits to regulate L-type calcium current kinetics and expression.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: