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PtdIns(4,5)P2 interacts with CaM binding domains on TRPM3 N-terminus
B. Holendova, L. Grycova, M. Jirku, J. Teisinger,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Free Medical Journals
from 2008 to 1 year ago
PubMed Central
from 2007
Europe PubMed Central
from 2007 to 1 year ago
Medline Complete (EBSCOhost)
from 2011-01-01
ROAD: Directory of Open Access Scholarly Resources
from 2007
PubMed
22989896
DOI
10.4161/chan.22177
Knihovny.cz E-resources
- MeSH
- Fluorescence Polarization MeSH
- Phosphatidylinositol 4,5-Diphosphate metabolism MeSH
- Calmodulin metabolism MeSH
- TRPM Cation Channels chemistry metabolism MeSH
- Liposomes metabolism MeSH
- Models, Molecular MeSH
- Surface Plasmon Resonance MeSH
- S100 Proteins metabolism MeSH
- Protein Structure, Tertiary MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
TRPM3 has been reported to play an important role in Ca(2+) homeostasis, but its gating mechanisms and regulation via Ca(2+) are unknown. Ca(2+) binding proteins such as calmodulin (CaM) could be probable modulators of this ion channel. We have shown that this protein binds to two independent domains, A35-K124 and H291-G382 on the TRPM3 N-terminus, which contain conserved hydrophobic as well as positively charged residues in specific positions, and that these residues have a crucial impact on its binding. We also showed that the other Ca(2+) binding protein, S100A1, is able to bind to these regions and that CaM and S100A1 compete for these binding sites on the TRPM3 N-terminus. Moreover, our results suggest that another very important TRP channel activity modulator, PtdIns(4,5)P(2), interacts with the CaM/S100A1 binding sites on the TRPM3 N-terminus with high affinity.
References provided by Crossref.org
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