The structure of lipid nanodisc-reconstituted TRPV3 reveals the gating mechanism
Transient receptor potential vanilloid subfamily member 3 (TRPV3) is a temperature-sensitive cation channel. Previous cryo-EM analyses of TRPV3 in detergent micelles or amphipol proposed that the lower gate opens by α-to-π helical transitions of the nearby S6 helix. However, it remains unclear how p...
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| Vydáno v: | Nature structural & molecular biology Ročník 27; číslo 7; s. 645 - 652 |
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| Hlavní autoři: | , , , , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
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United States
Nature Publishing Group
01.07.2020
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| ISSN: | 1545-9993, 1545-9985, 1545-9985 |
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| Abstract | Transient receptor potential vanilloid subfamily member 3 (TRPV3) is a temperature-sensitive cation channel. Previous cryo-EM analyses of TRPV3 in detergent micelles or amphipol proposed that the lower gate opens by α-to-π helical transitions of the nearby S6 helix. However, it remains unclear how physiological lipids are involved in the TRPV3 activation. Here we determined the apo state structure of mouse (Mus musculus) TRPV3 in a lipid nanodisc at 3.3 Å resolution. The structure revealed that lipids bound to the pore domain stabilize the selectivity filter in the narrow state, suggesting that the selectivity filter of TRPV3 affects cation permeation. When the lower gate is closed in nanodisc-reconstituted TRPV3, the S6 helix adopts the π-helical conformation without agonist- or heat-sensitization, potentially stabilized by putative intra-subunit hydrogen bonds and lipid binding. Our findings provide insights into the lipid-associated gating mechanism of TRPV3. |
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| AbstractList | Transient receptor potential vanilloid subfamily member 3 (TRPV3) is a temperature-sensitive cation channel. Previous cryo-EM analyses of TRPV3 in detergent micelles or amphipol proposed that the lower gate opens by α-to-π helical transitions of the nearby S6 helix. However, it remains unclear how physiological lipids are involved in the TRPV3 activation. Here we determined the apo state structure of mouse (Mus musculus) TRPV3 in a lipid nanodisc at 3.3 Å resolution. The structure revealed that lipids bound to the pore domain stabilize the selectivity filter in the narrow state, suggesting that the selectivity filter of TRPV3 affects cation permeation. When the lower gate is closed in nanodisc-reconstituted TRPV3, the S6 helix adopts the π-helical conformation without agonist- or heat-sensitization, potentially stabilized by putative intra-subunit hydrogen bonds and lipid binding. Our findings provide insights into the lipid-associated gating mechanism of TRPV3.A cryo-EM structure of mouse TRPV3 in nanodiscs reveal lipids bound to the pore domain, stabilizing the selectivity filter in the narrow state and the S6 in a π-helical conformation. Transient receptor potential vanilloid subfamily member 3 (TRPV3) is a temperature-sensitive cation channel. Previous cryo-EM analyses of TRPV3 in detergent micelles or amphipol proposed that the lower gate opens by α-to-π helical transitions of the nearby S6 helix. However, it remains unclear how physiological lipids are involved in the TRPV3 activation. Here we determined the apo state structure of mouse (Mus musculus) TRPV3 in a lipid nanodisc at 3.3 Å resolution. The structure revealed that lipids bound to the pore domain stabilize the selectivity filter in the narrow state, suggesting that the selectivity filter of TRPV3 affects cation permeation. When the lower gate is closed in nanodisc-reconstituted TRPV3, the S6 helix adopts the π-helical conformation without agonist- or heat-sensitization, potentially stabilized by putative intra-subunit hydrogen bonds and lipid binding. Our findings provide insights into the lipid-associated gating mechanism of TRPV3. Transient receptor potential vanilloid subfamily member 3 (TRPV3) is a temperature-sensitive cation channel. Previous cryo-EM analyses of TRPV3 in detergent micelles or amphipol proposed that the lower gate opens by α-to-π helical transitions of the nearby S6 helix. However, it remains unclear how physiological lipids are involved in the TRPV3 activation. Here we determined the apo state structure of mouse (Mus musculus) TRPV3 in a lipid nanodisc at 3.3 Å resolution. The structure revealed that lipids bound to the pore domain stabilize the selectivity filter in the narrow state, suggesting that the selectivity filter of TRPV3 affects cation permeation. When the lower gate is closed in nanodisc-reconstituted TRPV3, the S6 helix adopts the π-helical conformation without agonist- or heat-sensitization, potentially stabilized by putative intra-subunit hydrogen bonds and lipid binding. Our findings provide insights into the lipid-associated gating mechanism of TRPV3.Transient receptor potential vanilloid subfamily member 3 (TRPV3) is a temperature-sensitive cation channel. Previous cryo-EM analyses of TRPV3 in detergent micelles or amphipol proposed that the lower gate opens by α-to-π helical transitions of the nearby S6 helix. However, it remains unclear how physiological lipids are involved in the TRPV3 activation. Here we determined the apo state structure of mouse (Mus musculus) TRPV3 in a lipid nanodisc at 3.3 Å resolution. The structure revealed that lipids bound to the pore domain stabilize the selectivity filter in the narrow state, suggesting that the selectivity filter of TRPV3 affects cation permeation. When the lower gate is closed in nanodisc-reconstituted TRPV3, the S6 helix adopts the π-helical conformation without agonist- or heat-sensitization, potentially stabilized by putative intra-subunit hydrogen bonds and lipid binding. Our findings provide insights into the lipid-associated gating mechanism of TRPV3. |
| Author | Tominaga, Makoto Nureki, Osamu Dung Nguyen, T H Nishizawa, Tomohiro Shimada, Hiroto Hino, Tomoya Kusakizako, Tsukasa |
| Author_xml | – sequence: 1 givenname: Hiroto surname: Shimada fullname: Shimada, Hiroto organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo, Japan – sequence: 2 givenname: Tsukasa orcidid: 0000-0002-6186-6647 surname: Kusakizako fullname: Kusakizako, Tsukasa organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo, Japan – sequence: 3 givenname: T H surname: Dung Nguyen fullname: Dung Nguyen, T H organization: Division of Cell Signaling, National Institute for Physiological Sciences, National Institute of Natural Sciences, Okazaki, Japan – sequence: 4 givenname: Tomohiro orcidid: 0000-0001-7463-8398 surname: Nishizawa fullname: Nishizawa, Tomohiro organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo, Japan – sequence: 5 givenname: Tomoya orcidid: 0000-0002-8813-4622 surname: Hino fullname: Hino, Tomoya organization: Center for Research on Green Sustainable Chemistry, Tottori University, Tottori, Japan – sequence: 6 givenname: Makoto orcidid: 0000-0003-3111-3772 surname: Tominaga fullname: Tominaga, Makoto organization: Division of Cell Signaling, National Institute for Physiological Sciences, National Institute of Natural Sciences, Okazaki, Japan – sequence: 7 givenname: Osamu orcidid: 0000-0003-1813-7008 surname: Nureki fullname: Nureki, Osamu email: nureki@bs.s.u-tokyo.ac.jp organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo, Japan. nureki@bs.s.u-tokyo.ac.jp |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32572254$$D View this record in MEDLINE/PubMed |
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| Snippet | Transient receptor potential vanilloid subfamily member 3 (TRPV3) is a temperature-sensitive cation channel. Previous cryo-EM analyses of TRPV3 in detergent... |
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| SubjectTerms | Cations Channel gating Conformation Cryoelectron Microscopy Domains Hydrogen Bonding Hydrogen bonds Ion Channel Gating - physiology Ion channels Ions Lipids Lipids - chemistry Micelles Models, Molecular Nanostructures - chemistry Protein Conformation Selectivity Transient receptor potential proteins TRPV Cation Channels - chemistry TRPV Cation Channels - metabolism |
| Title | The structure of lipid nanodisc-reconstituted TRPV3 reveals the gating mechanism |
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