FRET analysis of the temperature-induced structural changes in human TRPV3
Abstract Transient receptor potential vanilloid member 3 (TRPV3) is an ion channel that plays a critical role in temperature sensing in skin. There have been active studies on how TRPV3, which is also known as one of the temperature-sensitive transient receptor potential (thermoTRP) channels, respon...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2023-06-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-023-36885-9 |
| _version_ | 1797795706480623616 |
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| author | Jinyoung Kim Jongdae Won Dong Kyu Chung Hyung Ho Lee |
| author_facet | Jinyoung Kim Jongdae Won Dong Kyu Chung Hyung Ho Lee |
| author_sort | Jinyoung Kim |
| collection | DOAJ |
| description | Abstract Transient receptor potential vanilloid member 3 (TRPV3) is an ion channel that plays a critical role in temperature sensing in skin. There have been active studies on how TRPV3, which is also known as one of the temperature-sensitive transient receptor potential (thermoTRP) channels, responds to temperature. However, the previous studies were mostly based on TRPV3 originating from mice or rats. Here, we focus on human TRPV3 (hTRPV3) and show that which domain of hTRPV3 undergoes conformational changes as temperature increases by Förster resonance energy transfer (FRET) assay. During the heat-induced activation of hTRPV3, the linker domain close to C-terminus, that is, the C-terminal domain shows a largest structural change whereas there is little change in the ankyrin repeat domain (ARD). Interestingly, the activation of hTRPV3 by an agonist shows structural change patterns that are completely different from those observed during activation by heat; we observe structural changes in ARD and S2–S3 linker after ligand stimulation whereas relatively little change is observed when stimulated by heat. Our results provide insight into the thermal activation of hTRPV3 channel. |
| first_indexed | 2024-03-13T03:22:04Z |
| format | Article |
| id | doaj.art-4e10289701d94719a8c16dc708d048ac |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-03-13T03:22:04Z |
| publishDate | 2023-06-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-4e10289701d94719a8c16dc708d048ac2023-06-25T11:17:12ZengNature PortfolioScientific Reports2045-23222023-06-011311810.1038/s41598-023-36885-9FRET analysis of the temperature-induced structural changes in human TRPV3Jinyoung Kim0Jongdae Won1Dong Kyu Chung2Hyung Ho Lee3Department of Chemistry, College of Natural Sciences, Seoul National UniversityDepartment of Chemistry, College of Natural Sciences, Seoul National UniversityDepartment of Chemistry, College of Natural Sciences, Seoul National UniversityDepartment of Chemistry, College of Natural Sciences, Seoul National UniversityAbstract Transient receptor potential vanilloid member 3 (TRPV3) is an ion channel that plays a critical role in temperature sensing in skin. There have been active studies on how TRPV3, which is also known as one of the temperature-sensitive transient receptor potential (thermoTRP) channels, responds to temperature. However, the previous studies were mostly based on TRPV3 originating from mice or rats. Here, we focus on human TRPV3 (hTRPV3) and show that which domain of hTRPV3 undergoes conformational changes as temperature increases by Förster resonance energy transfer (FRET) assay. During the heat-induced activation of hTRPV3, the linker domain close to C-terminus, that is, the C-terminal domain shows a largest structural change whereas there is little change in the ankyrin repeat domain (ARD). Interestingly, the activation of hTRPV3 by an agonist shows structural change patterns that are completely different from those observed during activation by heat; we observe structural changes in ARD and S2–S3 linker after ligand stimulation whereas relatively little change is observed when stimulated by heat. Our results provide insight into the thermal activation of hTRPV3 channel.https://doi.org/10.1038/s41598-023-36885-9 |
| spellingShingle | Jinyoung Kim Jongdae Won Dong Kyu Chung Hyung Ho Lee FRET analysis of the temperature-induced structural changes in human TRPV3 Scientific Reports |
| title | FRET analysis of the temperature-induced structural changes in human TRPV3 |
| title_full | FRET analysis of the temperature-induced structural changes in human TRPV3 |
| title_fullStr | FRET analysis of the temperature-induced structural changes in human TRPV3 |
| title_full_unstemmed | FRET analysis of the temperature-induced structural changes in human TRPV3 |
| title_short | FRET analysis of the temperature-induced structural changes in human TRPV3 |
| title_sort | fret analysis of the temperature induced structural changes in human trpv3 |
| url | https://doi.org/10.1038/s41598-023-36885-9 |
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