The self-association of two N-terminal interaction domains plays an important role in the tetramerization of TRPC4

被引：13

作者：

Lepage, Pascale K. ^{[1
]}

Lussier, Marc P. ^{[1
]}

McDuff, Francois-Olivier ^{[1
]}

Lavigne, Pierre ^{[1
]}

Boulay, Guylain ^{[1
]}

机构：

[1] Univ Sherbrooke, Fac Med & Hlth Sci, Dept Pharmacol, Sherbrooke, PQ J1H 5N4, Canada

来源：

CELL CALCIUM | 2009年 / 45卷 / 03期

基金：

加拿大健康研究院;

关键词：

TRPC; Tetramerization; Calcium signaling; Channel; Domain; ANKYRIN REPEAT DOMAIN; RECEPTOR POTENTIAL CHANNELS; CRYSTAL-STRUCTURE; CATION CHANNELS; K+ CHANNEL; PROTEINS; CALCIUM; NOMENCLATURE; TRAFFICKING; SUPERFAMILY;

D O I：

10.1016/j.ceca.2008.11.002

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Transient receptor potential canonical (TRPC) channels function as cation channels. In a previous study, we identified the molecular determinants involved in promoting TRPC subunit assembly. In the present study, we used size-exclusion chromatography assays to show that the N-terminus of TRPC4 can self-associate and form a tetramer in cellulo. We further showed that the N-terminus of TRPC4 self-associates via the ankyrin repeat domain and the region downstream from the coiled-coil domain. GST pull-down, yeast two-hybrid, and circular dichroism approaches demonstrated that both domains can self-associate. These findings indicated that the self-association of two distinct domains in the N-terminus of TRPC4 is involved in the assembly of the tetrameric channel. (c) 2008 Elsevier Ltd. All rights reserved.

引用

页码：251 / 259

页数：9

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