Conserved Residues within the Putative S4–S5 Region Serve Distinct Functions among Thermosensitive Vanilloid Transient Receptor Potential (TRPV) Channels

0354172 - FGÚ 2011 RIV US eng J - Journal Article
Boukalová, Štěpána - Maršáková, Lenka - Teisinger, Jan - Vlachová, Viktorie
Conserved Residues within the Putative S4–S5 Region Serve Distinct Functions among Thermosensitive Vanilloid Transient Receptor Potential (TRPV) Channels.
Journal of Biological Chemistry. Roč. 285, č. 53 (2010), s. 41455-41462. ISSN 0021-9258. E-ISSN 1083-351X
R&D Projects: GA ČR GA305/09/0081; GA ČR GAP301/10/1159; GA AV ČR(CZ) IAA600110701; GA MŠMT(CZ) 1M0517; GA MŠMT(CZ) LC554
Grant - others:Univerzita Karlova(CZ) 26110
Institutional research plan: CEZ:AV0Z50110509
Keywords : vanilloid receptor * voltage sensor * transient receptor potential
Subject RIV: FH - Neurology
Impact factor: 5.328, year: 2010

Based on the structural similarity to voltage-gated potassium channels, the voltage-sensing domain in the TRP channels is hypothesized to be comprised of positively charged amino acids distributed within the transmembrane segments S1-S4. Our data provide the first functional evidence that, despite the highly conserved nature of S4 and the S4-S5 linker, the mechanisms of temperature and chemical sensitivity in TRPV1 appear to utilize different residues from those in TRPV2 and TRPV3, which indicates that these mechanisms are not fully conserved throughout thermosensitive TRPV channels. This conclusion is further supported by our finding that one specific mode of chemical activation of TRPV1 is separable from other activation mechanisms and depends on one basic residue in the S4/S4-S5 domain
Permanent Link: http://hdl.handle.net/11104/0193233