Title |
T-type calcium channels functionally interact with spectrin (α/β) and ankyrin B
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Published in |
Molecular Brain, May 2018
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DOI | 10.1186/s13041-018-0368-5 |
Pubmed ID | |
Authors |
Agustin Garcia-Caballero, Fang-Xiong Zhang, Victoria Hodgkinson, Junting Huang, Lina Chen, Ivana A. Souza, Stuart Cain, Jennifer Kass, Sascha Alles, Terrance P. Snutch, Gerald W. Zamponi |
Abstract |
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. |
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