Homodimerization of the Src homology 3 domain of the calcium channel β-subunit drives dynamin-dependent endocytosis.

ABSTRACT: Voltage-dependent calcium channels constitute the main entry pathway for calcium into excitable cells. They are heteromultimers formed by an α(1) pore-forming subunit (Ca(V)α(1)) and accessory subunits. To achieve a precise coordination of calcium signals, the expression and activity of these channels is tightly controlled. The accessory β-subunit (Ca(V)β), a membrane associated guanylate kinase containing one guanylate kinase (β-GK) and one Src homology 3 (β-SH3) domain, has antagonistic effects on calcium currents by regulating different aspects of channel function. Although β-GK binds to a conserved site within the α(1)-pore-forming subunit and facilitates channel opening, β-SH3 binds to dynamin and promotes endocytosis. Here, we investigated the molecular switch underlying the function

SUBMITTER: Miranda-Laferte E 

PROVIDER: S-EPMC3121365 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature