Cryo-EM structure of TMEM63C suggests it functions as a monomer

Yuqi Qin, Daqi Yu, Dan Wu, Jiangqing Dong, William Thomas Li, Chang Ye, Kai Chit Cheung, Yingyi Zhang, Yun Xu, YongQiang Wang (), Yun Stone Shi () and Shangyu Dang ()
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Yuqi Qin: The Hong Kong University of Science and Technology, Clear Water Bay
Daqi Yu: The Hong Kong University of Science and Technology, Clear Water Bay
Dan Wu: Nanjing University
Jiangqing Dong: The Hong Kong University of Science and Technology, Clear Water Bay
William Thomas Li: The Hong Kong University of Science and Technology, Clear Water Bay
Chang Ye: Nanjing University
Kai Chit Cheung: The Hong Kong University of Science and Technology, Clear Water Bay
Yingyi Zhang: The Hong Kong University of Science and Technology, Clear Water Bay
Yun Xu: Nanjing University
YongQiang Wang: University of California
Yun Stone Shi: Nanjing University
Shangyu Dang: The Hong Kong University of Science and Technology, Clear Water Bay

Nature Communications, 2023, vol. 14, issue 1, 1-10

Abstract: Abstract The TMEM63 family proteins (A, B, and C), calcium-permeable channels in animals that are preferentially activated by hypo-osmolality, have been implicated in various physiological functions. Deficiency of these channels would cause many diseases including hearing loss. However, their structures and physiological roles are not yet well understood. In this study, we determine the cryo-electron microscopy (cryo-EM) structure of the mouse TMEM63C at 3.56 Å, and revealed structural differences compared to TMEM63A, TMEM63B, and the plant orthologues OSCAs. Further structural guided mutagenesis and calcium imaging demonstrated the important roles of the coupling of TM0 and TM6 in channel activity. Additionally, we confirm that TMEM63C exists primarily as a monomer under physiological conditions, in contrast, TMEM63B is a mix of monomer and dimer in cells, suggesting that oligomerization is a regulatory mechanism for TMEM63 proteins.

Date: 2023
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DOI: 10.1038/s41467-023-42956-2

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