Journal
CELL CALCIUM
Volume 45, Issue 3, Pages 251-259Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.ceca.2008.11.002
Keywords
TRPC; Tetramerization; Calcium signaling; Channel; Domain
Categories
Funding
- Canadian Institutes of Health Research
- Quebec Heart & Stroke Foundation
- Fonds de Recherche en Sante du Quebec
- Canadian Heart & Stroke Foundation
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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.
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