Asymmetric pendrin homodimer reveals its molecular mechanism as anion exchanger

Qianying Liu, Xiang Zhang, Hui Huang, Yuxin Chen, Fang Wang, Aihua Hao, Wuqiang Zhan, Qiyu Mao, Yuxia Hu, Lin Han, Yifang Sun, Meng Zhang, Zhimin Liu, Geng-Lin Li, Weijia Zhang, Yilai Shu (), Lei Sun () and Zhenguo Chen ()
Additional contact information
Qianying Liu: Fudan University
Xiang Zhang: Fudan University
Hui Huang: Fudan University
Yuxin Chen: Fudan University
Fang Wang: Fudan University
Aihua Hao: Fudan University
Wuqiang Zhan: Fudan University
Qiyu Mao: Fudan University
Yuxia Hu: Fudan University
Lin Han: Fudan University
Yifang Sun: Fudan University
Meng Zhang: Fudan University
Zhimin Liu: Fudan University
Geng-Lin Li: Fudan University
Weijia Zhang: Fudan University
Yilai Shu: Fudan University
Lei Sun: Fudan University
Zhenguo Chen: Fudan University

Nature Communications, 2023, vol. 14, issue 1, 1-11

Abstract: Abstract Pendrin (SLC26A4) is an anion exchanger expressed in the apical membranes of selected epithelia. Pendrin ablation causes Pendred syndrome, a genetic disorder associated with sensorineural hearing loss, hypothyroid goiter, and reduced blood pressure. However its molecular structure has remained unknown, limiting our understanding of the structural basis of transport. Here, we determine the cryo-electron microscopy structures of mouse pendrin with symmetric and asymmetric homodimer conformations. The asymmetric homodimer consists of one inward-facing protomer and the other outward-facing protomer, representing coincident uptake and secretion- a unique state of pendrin as an electroneutral exchanger. The multiple conformations presented here provide an inverted alternate-access mechanism for anion exchange. The structural and functional data presented here disclose the properties of an anion exchange cleft and help understand the importance of disease-associated variants, which will shed light on the pendrin exchange mechanism.

Date: 2023
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-38303-0

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DOI: 10.1038/s41467-023-38303-0

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