Ion channels and transports are integral membrane proteins that mediate the flow of ions across the membrane. Ion channels are activated by electric potential gradient or ligands, and transporters normally undergo large conformational changes to conduct ions. Ryanodine receptors (RYRs), a class of calcium channels that release calcium from cellular organelles, is the first ion channel we worked on, through the collaboration with Nieng Yan lab. We managed to determine the high resolution cryo-EM structures of RYR1 in both close and open states. After moving to UTSW, we established a close collaboration with Youxing Jiang lab, working on different types of ion channels and transporters. In the past few years, we were able to solve the cryo-EM structures of several important ion channels, including TRPML1, TRPM4, TPC, and MCU. These structural studies shed light on the activation mechanisms of these ion channels. We are currently working on the structural and functional studies of several other voltage-gated ion channels and transporters that are closely related to human diseases.

Collaborator

Youxing Jiang

Related Publications

Yan Wang, Nam X Nguyen, Ji She, Weizhong Zeng, Yi Yang, Xiao-chen Bai†, Youxing Jiang†. Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter. Cell, VOLUME 177, ISSUE 5, P1252-1261.E13, MAY 16, 2019.

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Qingfeng Chen, Weizhong Zeng, Ji She, Xiao-chen Bai†, Youxing Jiang†. Structural and functional characterization of an otopetrin family proton channel. eLife 2019;8:e46710.

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Ji She, Weizhong Zeng, Jiangtao Guo, Qingfeng Chen, Xiao-chen Bai†, Youxing Jiang†. Structural mechanisms of phospholipid activation of the human TPC2 channel. eLife 2019;8:e45222.

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Nam X. Nguyen, Jean-Paul Armache, Changkeun Lee, Yi Yang, Weizhong Zeng, Vamsi K. Mootha, Yifan Cheng, Xiao-chen Bai†, Youxing Jiang†. Cryo-EM structure of a fungal mitochondrial calcium uniporter. Nature volume 559, pages 570–574 (2018).

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Ji She*, Jiangtao Guo*, Qingfeng Chen*, Weizhong Zeng , Youxing Jiang†, Xiao-chen Bai†. Structural insights into the voltage and phospholipid activation of the mammalian TPC1 channel. Nature volume 556, pages 130–134 (05 April 2018).

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Jiangtao Guo*, Ji She*, Weizhong Zeng, Qingfeng Chen, Xiao-chen Bai†, Youxing Jiang†. Structures of the calcium-activated, non-selective cation channel TRPM4. Nature volume 552, pages 205–209 (14 December 2017).

[DOI]

Qingfeng Chen*, Ji She*, Weizhong Zeng, Jiangtao Guo, Haoxing Xu, Xiao-chen Bai†, Youxing Jiang†.. Structure of mammalian endolysosomal TRPML1 channel in nanodiscs. Nature volume 550, pages 415–418 (19 October 2017).

[DOI]

Xiao-chen Bai*, Zhen Yan†*, Jianping Wu*, Zhangqiang Li, Nieng Yan†. The Central domain of RyR1 is the transducer for long-range allosteric gating of channel opening. Cell Research volume 26, pages 995–1006 (2016).

[DOI]

Zhen Yan*, Xiao-chen Bai*, Chuangye Yan*, JianpingWu, Zhangqiang Li, TianXie,Wei Peng, Chang-cheng Yin, Xueming Li, Sjors H. W. Scheres†, Yigong Shi†, Nieng Yan†. Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution. Nature volume 517, pages 50–55 (01 January 2015).

[DOI]