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-Structure paper
タイトル | Regulatory switch at the cytoplasmic interface controls TRPV channel gating. |
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ジャーナル・号・ページ | Elife, Vol. 8, Year 2019 |
掲載日 | 2019年5月9日 |
著者 | Lejla Zubcevic / William F Borschel / Allen L Hsu / Mario J Borgnia / Seok-Yong Lee / |
PubMed 要旨 | Temperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels are activated by ligands and heat, and are involved in various physiological processes. ThermoTRPV channels possess ...Temperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels are activated by ligands and heat, and are involved in various physiological processes. ThermoTRPV channels possess a large cytoplasmic ring consisting of N-terminal ankyrin repeat domains (ARD) and C-terminal domains (CTD). The cytoplasmic inter-protomer interface is unique and consists of a CTD coiled around a β-sheet which makes contacts with the neighboring ARD. Despite much existing evidence that the cytoplasmic ring is important for thermoTRPV function, the mechanism by which this unique structure is involved in thermoTRPV gating has not been clear. Here, we present cryo-EM and electrophysiological studies which demonstrate that TRPV3 gating involves large rearrangements at the cytoplasmic inter-protomer interface and that this motion triggers coupling between cytoplasmic and transmembrane domains, priming the channel for opening. Furthermore, our studies unveil the role of this interface in the distinct biophysical and physiological properties of individual thermoTRPV subtypes. |
リンク | Elife / PubMed:31070581 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.6 - 4.1 Å |
構造データ | EMDB-20192: Structure of the TRPV3 K169A sensitized mutant in apo form at 4.1 A resolution. EMDB-20194, PDB-6ot5: |
化合物 | ChemComp-FZ4: |
由来 |
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キーワード | TRANSPORT PROTEIN (運搬体タンパク質) / Ion channel (イオンチャネル) / TRP channel (TRPチャネル) / TRPV channel / Metal transport / Membrane transport / membrane protein (膜タンパク質) |