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Neurochem Int. 2010 Jan;56(2):363-6. doi: 10.1016/j.neuint.2009.11.009. Epub 2009 Nov 20.

The interactions of the C-terminal region of the TRPC6 channel with calmodulin.

Author information

1
Institute of Physiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic.

Abstract

The transient receptor potential channel TRPC6 is a non-selective cation channel which modulates the calcium level in eukaryotic cells (including sensory receptor cells) in response to external signals. Calmodulin (CaM) is a ubiquitously expressed Ca(2+) binding protein that is an important mediator of Ca(2+)-dependent regulation of the TRPC6 channel. One CaM binding site was identified within the C-tail of TRPC6. The aim of this study is to map in detail the CaM and inositol (1,4,5)-triphosphate receptor binding (CIRB) domain in the C-terminal region of mouse TRPC6 that is capable of interacting with CaM using in vitro binding assays. Besides the set of positively charged amino acid residues Arg852, Lys856, Arg864, Lys859/Arg860, a hydrophobic Ile857, at the position 1 in 1-5-10 motif, was located and the effect of replacing it with a neutral residue was tested using fluorescence anisotropy measurement. Participation of Ile857 could indicate a strong role of this conserved CaM binding motif.

PMID:
19932145
DOI:
10.1016/j.neuint.2009.11.009
[Indexed for MEDLINE]

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