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Putative interaction site for membrane phospholipids controls activation of TRPA1 channel at physiological membrane potentials

dc.rights.licenseopenen_US
dc.contributor.authorMACIKOVA, Lucie
dc.contributor.authorSINICA, Viktor
dc.contributor.authorKADKOVA, Anna
dc.contributor.authorVILLETTE, Sandrine
dc.contributor.authorCIACCAFAVA, Alexandre
dc.contributor.authorFAHERTY, Jonathan
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLECOMTE, Sophie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorALVES, Isabel
dc.contributor.authorVLACHOVA, Viktorie
dc.date.accessioned2020-05-12T08:36:47Z
dc.date.available2020-05-12T08:36:47Z
dc.date.issued2019
dc.identifier.issn1742-464Xen_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/7543
dc.description.abstractEnThe transient receptor potential ankyrin 1 (TRPA1) channel is a polymodal sensor of environmental irritant compounds, endogenous proalgesic agents, and cold. Upon activation, TRPA1 channels increase cellular calcium levels via direct permeation and trigger signaling pathways that hydrolyze phosphatidylinositol-4,5-bisphosphate (PIP2 ) in the inner membrane leaflet. Our objective was to determine the extent to which a putative PIP2 -interaction site (Y1006-Q1031) is involved in TRPA1 regulation. The interactions of two specific peptides (L992-N1008 and T1003-P1034) with model lipid membranes were characterized by biophysical approaches to obtain information about affinity, peptide secondary structure, and peptide effect in the lipid organization. The results indicate that the two peptides interact with lipid membranes only if PIP2 is present and their affinities depend on the presence of calcium. Using whole-cell electrophysiology, we demonstrate that mutation at F1020 produced channels with faster activation kinetics and with a rightward shifted voltage-dependent activation curve by altering the allosteric constant that couples voltage sensing to pore opening. We assert that the presence of PIP2 is essential for the interaction of the two peptide sequences with the lipid membrane. The putative phosphoinositide-interacting domain comprising the highly conserved F1020 contributes to the stabilization of the TRPA1 channel gate.
dc.language.isoENen_US
dc.subject.enankyrin transient receptor potential
dc.subject.engating
dc.subject.enpeptide–lipid interaction
dc.subject.enrectification
dc.subject.enTRP channel
dc.title.enPutative interaction site for membrane phospholipids controls activation of TRPA1 channel at physiological membrane potentials
dc.title.alternativefebsen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1111/febs.14931
dc.subject.halChimie/Matériauxen_US
bordeaux.journalThe FEBS journalen_US
bordeaux.page3664-3683en_US
bordeaux.volume286en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.issue18en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03184030
hal.version1
hal.date.transferred2021-03-29T08:49:36Z
hal.exporttrue
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