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
收藏
页码：251 / 259
页数：9
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