T-type calcium channels functionally interact with spectrin (α/β) and ankyrin B

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dc.contributor.authorGarcia-Caballero, Agustin
dc.contributor.authorZhang, Fang-Xiong
dc.contributor.authorHodgkinson, Victoria
dc.contributor.authorHuang, Junting
dc.contributor.authorChen, Lina
dc.contributor.authorSouza, Ivana A
dc.contributor.authorCain, Stuart
dc.contributor.authorKass, Jennifer
dc.contributor.authorAlles, Sascha
dc.contributor.authorSnutch, Terrance P
dc.contributor.authorZamponi, Gerald W
dc.date.accessioned2018-09-26T12:09:54Z
dc.date.available2018-09-26T12:09:54Z
dc.date.issued2018-05-02
dc.date.updated2018-09-26T12:09:53Z
dc.description.abstractAbstract 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.
dc.identifier.citationMolecular Brain. 2018 May 02;11(1):24
dc.identifier.doihttps://doi.org/10.1186/s13041-018-0368-5
dc.identifier.urihttp://hdl.handle.net/1880/108007
dc.identifier.urihttps://doi.org/10.11575/PRISM/45685
dc.language.rfc3066en
dc.rights.holderThe Author(s).
dc.titleT-type calcium channels functionally interact with spectrin (α/β) and ankyrin B
dc.typeJournal Article
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