1.1)State Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, Beijing 100871, China;2.2)Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China;3.3)Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, China
This work was supported by grants from the Ministry of Science and Technology of China (2016YFA0502004), The National Natural Science Foundation of China (91957201, 31622021, 31870833, 31821091), Beijing Natural Science Foundation (5192009) and Young Thousand Talents Program of China.
Hyperosmolality-induced [Ca2+]i increase (OSCA)/Transmembrane protein 63 (TMEM63) family proteins are multi-pass membrane proteins. They are broadly presented in eukaryotic cells. Previous study showed that OSCA1.1 from Arabidopsis mediated the hyperosmolality induced calcium increase in plants. Additional studies showed OSCA1.1 and its homologues were mechanosensitive ion channels. High resolution cryo-EM structures revealed that OSCA proteins were symmetric dimers and each subunit harbored an ion permeation pathway. The review will focus on recent progress on the studies of the function, structure and structural-functional relationship of OSCA channels.
WU Jing-Xiang, CHEN Lei. Recent Progress on The Studies of OSCA/TMEM63 Family Ion Channels[J]. Progress in Biochemistry and Biophysics,2020,47(2):123-130
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