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dc.contributor.authorMa, Linlin
dc.contributor.authorYang, Fan
dc.contributor.authorVu, Simon
dc.contributor.authorZheng, Jie
dc.date.accessioned2020-02-27T02:05:41Z
dc.date.available2020-02-27T02:05:41Z
dc.date.issued2016
dc.identifier.issn2045-2322
dc.identifier.doi10.1038/srep33827
dc.identifier.urihttp://hdl.handle.net/10072/391958
dc.description.abstractTRPV1 is a polymodal nociceptor for diverse physical and chemical stimuli that interact with different parts of the channel protein. Recent cryo-EM studies revealed detailed channel structures, opening the door for mapping structural elements mediating activation by each stimulus. Towards this goal, here we have combined unstructured peptide-insertion screening (UPS) with electrophysiological and fluorescence recordings to explore structural and functional roles of the intracellular regions of TRPV1 in mediating various activation stimuli. We found that most of the tightly packed protein regions did not tolerate structural perturbation by UPS when tested, indicating that structural integrity of the intracellular region is critical. In agreement with previous reports, Ca2+-dependent desensitization is strongly dependent on both intracellular N- and C-terminal domains; insertions of an unstructured peptide between these domains and the transmembrane core domain nearly eliminated Ca2+-dependent desensitization. In contrast, channel activations by capsaicin, low pH, divalent cations, and even heat are mostly intact in mutant channels containing the same insertions. These observations suggest that the transmembrane core domain of TRPV1, but not the intracellular domains, is responsible for sensing these stimuli.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherNature Publishing Group
dc.relation.ispartofissue1
dc.relation.ispartofjournalScientific Reports
dc.relation.ispartofvolume6
dc.subject.fieldofresearchProteomics and metabolomics
dc.subject.fieldofresearchcode310205
dc.subject.keywordsScience & Technology
dc.subject.keywordsMultidisciplinary Sciences
dc.subject.keywordsScience & Technology - Other Topics
dc.subject.keywordsCAPSAICIN RECEPTOR TRPV1
dc.subject.keywordsION-CHANNEL
dc.titleExploring functional roles of TRPV1 intracellular domains with unstructured peptide-insertion screening
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationMa, L; Yang, F; Vu, S; Zheng, J, Exploring functional roles of TRPV1 intracellular domains with unstructured peptide-insertion screening, Scientific Reports, 2016, 6 (1)
dcterms.dateAccepted2016-08-30
dcterms.licensehttp://creativecommons.org/licenses/by/4.0/
dc.date.updated2020-02-27T02:03:25Z
dc.description.versionVersion of Record (VoR)
gro.rights.copyright© The Author(s) 2016. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
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gro.griffith.authorMa, Linlin


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