Journal
NEUROCHEMISTRY INTERNATIONAL
Volume 56, Issue 2, Pages 363-366Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.neuint.2009.11.009
Keywords
TRPC6; Calmodulin; Fluorescence anisotropy
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Funding
- GAAV [IAA600110701]
- GACR [303/07/0915, GACRGA CR 305/08/H037]
- Ministry of Education, Youth, and Sports of the Czech Republic [MSM0021620857, LC554]
- Academy of Sciences of the Czech Republic [AVOZ 50110509]
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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 Ca2+ binding protein that is an important mediator of Ca2+-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. (C) 2009 Elsevier Ltd. All rights reserved.
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