TY - JOUR T1 - A common mechanism of temperature-sensing in thermoTRP channels JF - bioRxiv DO - 10.1101/2022.05.23.493163 SP - 2022.05.23.493163 AU - Lizhen Xu AU - Xiao Liang AU - Wenxuan Zhen AU - Zhangzhi Xue AU - Fangfei Zhang AU - Xiao Yi AU - Xiaoying Chen AU - Lidan Hu AU - Bei Li AU - Bing Zhang AU - Yuhang Wang AU - Zhenfeng Deng AU - Wei Yang AU - Han Wen AU - Tiannan Guo AU - Yi Zhu AU - Fan Yang Y1 - 2022/01/01 UR - http://biorxiv.org/content/early/2022/05/24/2022.05.23.493163.abstract N2 - 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. ER -