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

SYSNO ASEP	0354172
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Conserved Residues within the Putative S4–S5 Region Serve Distinct Functions among Thermosensitive Vanilloid Transient Receptor Potential (TRPV) Channels
Author(s)	Boukalová, Štěpána (FGU-C) Maršáková, Lenka (FGU-C)_RID Teisinger, Jan (FGU-C)_RID Vlachová, Viktorie (FGU-C)_{RID, ORCID, SAI}
Source Title	Journal of Biological Chemistry. - : Elsevier - ISSN 0021-9258 Roč. 285, č. 53 (2010), s. 41455-41462
Number of pages	8 s.
Language	eng - English
Country	US - United States
Keywords	vanilloid receptor ; voltage sensor ; transient receptor potential
Subject RIV	FH - Neurology
R&D Projects	GA305/09/0081 GA ČR - Czech Science Foundation (CSF)
	GAP301/10/1159 GA ČR - Czech Science Foundation (CSF)
	IAA600110701 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
	1M0517 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
	LC554 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
CEZ	AV0Z50110509 - FGU-C (2005-2011)
UT WOS	000285622600031
DOI	10.1074/jbc.M110.145466
Annotation	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
Workplace	Institute of Physiology
Contact	Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400
Year of Publishing	2011

Number of the records: 1