Functionally important amino acid residues in the transient receptor potential vanilloid 1 (TRPV1) ion channel--an overview of the current mutational data
- PMID: 23800232
- PMCID: PMC3707783
- DOI: 10.1186/1744-8069-9-30
Functionally important amino acid residues in the transient receptor potential vanilloid 1 (TRPV1) ion channel--an overview of the current mutational data
Abstract
This review aims to create an overview of the currently available results of site-directed mutagenesis studies on transient receptor potential vanilloid type 1 (TRPV1) receptor. Systematization of the vast number of data on the functionally important amino acid mutations of TRPV1 may provide a clearer picture of this field, and may promote a better understanding of the relationship between the structure and function of TRPV1. The review summarizes information on 112 unique mutated sites along the TRPV1, exchanged to multiple different residues in many cases. These mutations influence the effect or binding of different agonists, antagonists, and channel blockers, alter the responsiveness to heat, acid, and voltage dependence, affect the channel pore characteristics, and influence the regulation of the receptor function by phosphorylation, glycosylation, calmodulin, PIP2, ATP, and lipid binding. The main goal of this paper is to publish the above mentioned data in a form that facilitates in silico molecular modelling of the receptor by promoting easier establishment of boundary conditions. The better understanding of the structure-function relationship of TRPV1 may promote discovery of new, promising, more effective and safe drugs for treatment of neurogenic inflammation and pain-related diseases and may offer new opportunities for therapeutic interventions.
Figures
Similar articles
-
Ca(2+) binding protein S100A1 competes with calmodulin and PIP2 for binding site on the C-terminus of the TPRV1 receptor.ACS Chem Neurosci. 2015 Mar 18;6(3):386-92. doi: 10.1021/cn500250r. Epub 2014 Dec 31. ACS Chem Neurosci. 2015. PMID: 25543978
-
Conserved residues within the putative S4-S5 region serve distinct functions among thermosensitive vanilloid transient receptor potential (TRPV) channels.J Biol Chem. 2010 Dec 31;285(53):41455-62. doi: 10.1074/jbc.M110.145466. Epub 2010 Nov 2. J Biol Chem. 2010. PMID: 21044960 Free PMC article.
-
Conserved allosteric pathways for activation of TRPV3 revealed through engineering vanilloid-sensitivity.Elife. 2019 Jan 15;8:e42756. doi: 10.7554/eLife.42756. Elife. 2019. PMID: 30644819 Free PMC article.
-
TRPV1: Structure, Endogenous Agonists, and Mechanisms.Int J Mol Sci. 2020 May 12;21(10):3421. doi: 10.3390/ijms21103421. Int J Mol Sci. 2020. PMID: 32408609 Free PMC article. Review.
-
TRPV1.Handb Exp Pharmacol. 2014;222:207-45. doi: 10.1007/978-3-642-54215-2_9. Handb Exp Pharmacol. 2014. PMID: 24756708 Review.
Cited by
-
The pain receptor TRPV1 displays agonist-dependent activation stoichiometry.Sci Rep. 2015 Jul 21;5:12278. doi: 10.1038/srep12278. Sci Rep. 2015. PMID: 26194846 Free PMC article.
-
The role of TRPV1 ion channels in the suppression of gastric cancer development.J Exp Clin Cancer Res. 2020 Oct 2;39(1):206. doi: 10.1186/s13046-020-01707-7. J Exp Clin Cancer Res. 2020. PMID: 33008449 Free PMC article.
-
Myrcene and terpene regulation of TRPV1.Channels (Austin). 2019 Dec;13(1):344-366. doi: 10.1080/19336950.2019.1654347. Channels (Austin). 2019. PMID: 31446830 Free PMC article.
-
Understanding TRPV1 activation by ligands: Insights from the binding modes of capsaicin and resiniferatoxin.Proc Natl Acad Sci U S A. 2016 Jan 12;113(2):E137-45. doi: 10.1073/pnas.1517288113. Epub 2015 Dec 30. Proc Natl Acad Sci U S A. 2016. PMID: 26719417 Free PMC article.
-
Tyrosine Residue in the TRPV1 Vanilloid Binding Pocket Regulates Deactivation Kinetics.J Biol Chem. 2016 Jun 24;291(26):13855-63. doi: 10.1074/jbc.M116.726372. Epub 2016 May 3. J Biol Chem. 2016. PMID: 27143360 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources