RT Journal Article
SR Electronic
T1 A common mechanism of temperature-sensing in thermoTRP channels
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2022.05.23.493163
DO 10.1101/2022.05.23.493163
A1 Lizhen Xu
A1 Xiao Liang
A1 Wenxuan Zhen
A1 Zhangzhi Xue
A1 Fangfei Zhang
A1 Xiao Yi
A1 Xiaoying Chen
A1 Lidan Hu
A1 Bei Li
A1 Bing Zhang
A1 Yuhang Wang
A1 Zhenfeng Deng
A1 Wei Yang
A1 Han Wen
A1 Tiannan Guo
A1 Yi Zhu
A1 Fan Yang
YR 2022
UL http://biorxiv.org/content/early/2022/05/24/2022.05.23.493163.abstract
AB Detecting temperature is crucial for the survival of living organisms. Though the thermo transient receptor potential (thermoTRP) channels, such as TRPV1 or TRPM8, have been identified as prototypic heat or cold sensors, respectively, how they detect temperature remains elusive. Here we first identified groups of clustered residues in these channels that undergo burial/exposure conformational rearrangements during temperature activation by analyzing available protein structures or hydroxyl radical footprinting-mass spectroscopy (HRF-MS). By systematically perturbing water-protein interactions at these residues, we found that the temperature sensitivity in these channels were modulated in accordance with the sidechain hydrophobicity. The changes in energy associated with changes in water-protein interactions were sufficient for thermo activation. Therefore, our study has established that the water-protein interactions as a common mechanism underlying temperature sensing in TRPM8 and TRPV1.Competing Interest StatementThe authors have declared no competing interest.