journal article·2022-07-14

Extreme Membrane Tensile Loads Induce Half-Activation of the Thermosensitive TRPV1 Channel

Lingzhi Gu, Mi Zhou, Tong Wei, Hong Yang, Yang Zhou

Publisher page

Abstract

Transient receptor potential (TRP) channels are sensors for a wide range of cellular and environmental signals, but elucidating how these channels convert a wide range of physical and chemical stimuli into channel opening is essential to understanding their normal function. Here, half-activation of thermosensitive TRPV1 channel under extreme membrane stretching from blast loads was provided by molecular dynamics simulations. The results show that such extreme membrane stretch loading will only lead to half-activation of the TRPV1 channel: that is, the upper gate is open for high-speed stretching (>15m/s), but the lower gate is still closed. The corresponding activation threshold also depends on both the tensile speed and the area strain. This means that the direct mechanical gating of TRP channels in one step is unlikely to occur.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Ion Channels and Receptors · Plant and Biological Electrophysiology Studies

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Institute of Chemical Materials, China Academy of Engineering and Physics, Mianyang 621900, China

Funding

National Natural Science Foundation of China

References (34)

Show source-provided references
1. 10.1038/nature0219610.1038/nature02196 ↗
2. 10.1038/nchembio0705-8510.1038/nchembio0705-85 ↗
3. 10.1007/BF0053645510.1007/BF00536455 ↗
4. 10.1126/science.393311210.1126/science.3933112 ↗
5. 10.1038/nrn214910.1038/nrn2149 ↗
6. 10.1038/3980710.1038/39807 ↗
7. 10.1007/7355_2015_9810.1007/7355_2015_98 ↗
8. 10.1038/nrn114110.1038/nrn1141 ↗
9. 10.1016/S0092-8674(03)00158-210.1016/S0092-8674(03)00158-2 ↗
10. 10.1038/nn.258110.1038/nn.2581 ↗
11. 10.1016/S0896-6273(03)00505-110.1016/S0896-6273(03)00505-1 ↗
12. 10.1038/nn.255210.1038/nn.2552 ↗
13. 10.1073/pnas.151728811310.1073/pnas.1517288113 ↗
14. 10.1186/s12974-016-0738-910.1186/s12974-016-0738-9 ↗
15. 10.1016/j.bbrc.2015.02.06710.1016/j.bbrc.2015.02.067 ↗
16. 10.1016/j.tins.2012.03.00410.1016/j.tins.2012.03.004 ↗
17. 10.1007/978-3-319-05161-1_410.1007/978-3-319-05161-1_4 ↗
18. 10.3389/fneur.2013.0005910.3389/fneur.2013.00059 ↗
19. 10.1021/acs.jpclett.2c0032110.1021/acs.jpclett.2c00321 ↗
20. 10.1089/neu.2010.144210.1089/neu.2010.1442 ↗
21. 10.1021/acs.jpcb.1c0554410.1021/acs.jpcb.1c05544 ↗
22. 10.1016/j.jbiomech.2011.05.01410.1016/j.jbiomech.2011.05.014 ↗
23. 10.1038/srep1536910.1038/srep15369 ↗
24. 10.1002/prot.2517710.1002/prot.25177 ↗
25. 10.1016/j.bpj.2017.10.03410.1016/j.bpj.2017.10.034 ↗
26. 10.1080/23328940.2019.157863410.1080/23328940.2019.1578634 ↗
27. 10.1038/srep3311210.1038/srep33112 ↗
28. 10.1016/j.jtbi.2018.02.00410.1016/j.jtbi.2018.02.004 ↗
29. 10.1038/s41467-018-07117-w10.1038/s41467-018-07117-w ↗
30. 10.1038/nature1282210.1038/nature12822 ↗
31. 10.1038/nature1282310.1038/nature12823 ↗
32. 10.1146/annurev.biochem.75.103004.14281910.1146/annurev.biochem.75.103004.142819 ↗
33. 10.1021/acs.jpcb.9b0303310.1021/acs.jpcb.9b03033 ↗
34. 10.1016/j.bbamem.2011.07.02210.1016/j.bbamem.2011.07.022 ↗