The interactions of the C-terminal region of the TRPC6 channel with calmodulin
Language English Country Great Britain, England Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
19932145
DOI
10.1016/j.neuint.2009.11.009
PII: S0197-0186(09)00314-3
Knihovny.cz E-resources
- MeSH
- Fluorescence Polarization MeSH
- Calmodulin metabolism MeSH
- TRPC Cation Channels chemistry genetics metabolism MeSH
- TRPC6 Cation Channel MeSH
- Cloning, Molecular MeSH
- Models, Molecular MeSH
- Mutagenesis, Site-Directed MeSH
- Mice MeSH
- Electrophoretic Mobility Shift Assay MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Calmodulin MeSH
- TRPC Cation Channels MeSH
- TRPC6 Cation Channel MeSH
- Trpc6 protein, mouse MeSH Browser
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.
References provided by Crossref.org
Characterization of the S100A1 protein binding site on TRPC6 C-terminus
Integrative binding sites within intracellular termini of TRPV1 receptor
PtdIns(4,5)P2 interacts with CaM binding domains on TRPM3 N-terminus
Calmodulin and S100A1 protein interact with N terminus of TRPM3 channel
