Garcia-Caballero, AgustinZhang, Fang-XiongHodgkinson, VictoriaHuang, JuntingChen, LinaSouza, Ivana ACain, StuartKass, JenniferAlles, SaschaSnutch, Terrance PZamponi, Gerald W2018-09-262018-09-262018-05-02Molecular Brain. 2018 May 02;11(1):24http://hdl.handle.net/1880/108007https://doi.org/10.11575/PRISM/45685Abstract This study describes the functional interaction between the Cav3.1 and Cav3.2 T-type calcium channels and cytoskeletal spectrin (α/β) and ankyrin B proteins. The interactions were identified utilizing a proteomic approach to identify proteins that interact with a conserved negatively charged cytosolic region present in the carboxy-terminus of T-type calcium channels. Deletion of this stretch of amino acids decreased binding of Cav3.1 and Cav3.2 calcium channels to spectrin (α/β) and ankyrin B and notably also reduced T-type whole cell current densities in expression systems. Furthermore, fluorescence recovery after photobleaching analysis of mutant channels lacking the proximal C-terminus region revealed reduced recovery of both Cav3.1 and Cav3.2 mutant channels in hippocampal neurons. Knockdown of spectrin α and ankyrin B decreased the density of endogenous Cav3.2 in hippocampal neurons. These findings reveal spectrin (α/β) / ankyrin B cytoskeletal and signaling proteins as key regulators of T-type calcium channels expressed in the nervous system.Journal Article2018-09-26enThe Author(s).https://doi.org/10.1186/s13041-018-0368-5