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Cell Calcium. 2009 Mar;45(3):251-9. doi: 10.1016/j.ceca.2008.11.002. Epub 2008 Dec 12.

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

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  • 1Department of Pharmacology, Université de Sherbrooke, Sherbrooke, Quebec, Canada.

Abstract

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.

PMID:
19070363
[PubMed - indexed for MEDLINE]
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