Regulation of CaV3.2 channels by the receptor for activated C kinase 1 (Rack-1)

被引：6

作者：

Gandini, Maria A. ^{[1
,2
]}

Souza, Ivana A. ^{[1
,2
]}

Kullar, Abhishek ^{[1
,2
]}

Gambeta, Eder ^{[1
,2
]}

Zamponi, Gerald W. ^{[1
,2
]}

机构：

[1] Univ Calgary, Dept Physiol & Pharmacol, Hotchkiss Brain Inst, Calgary, AB, Canada

[2] Univ Calgary, Alberta Childrens Hosp Res Inst, Cumming Sch Med, Calgary, AB, Canada

来源：

PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY | 2022年 / 474卷 / 04期

基金：

加拿大健康研究院;

关键词：

PKC; T-type channels; Pain; Rack-1; CALCIUM-CHANNELS; BETA-II; SCAFFOLDING PROTEIN; SENSORY NEURONS; UP-REGULATION; PAIN; PHOSPHORYLATION; GLYCOSYLATION; EXPRESSION; SUBUNIT;

D O I：

10.1007/s00424-021-02631-1

中图分类号：

Q4 [生理学];

学科分类号：

071003 ;

摘要：

This study describes the interaction between Ca(V)3.2 calcium channels and the receptor for activated C kinase 1 (Rack-1), a scaffold protein which has recently been implicated in neuropathic pain. The coexpression of Ca(V)3.2 and Rack-1 in tsA-201 cells led to a reduction in the magnitude of whole-cell Ca(V)3.2 currents and Ca(V)3.2 channel expression at the plasma membrane. Co-immunoprecipitations from transfected cells show the formation of a molecular protein complex between Cav3.2 channels and Rack-1. We determined that the interaction of Rack-1 occurs at the intracellular II-III loop and the C-terminus of the channel. Finally, the coexpression of PKC beta II abolished the effect of Rack-1 on current densities. Altogether, our findings show that Rack-1 regulates Ca(V)3.2-mediated calcium entry in a PKC-dependent manner.

引用

页码：447 / 454

页数：8

共 43 条

[1] RACK1, A multifaceted scaffolding protein: Structure and function [J].