Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis

Yaming Lu, Miao Yu, Yutian Jia, Fan Yang, Yanming Zhang, Xia Xu, Xiaomin Li, Fan Yang, Jianlin Lei, Yi Wang () and Guanghui Yang ()
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Yaming Lu: China Agricultural University
Miao Yu: China Agricultural University
Yutian Jia: China Agricultural University
Fan Yang: China Agricultural University
Yanming Zhang: China Agricultural University
Xia Xu: China Agricultural University
Xiaomin Li: Tsinghua University
Fan Yang: Tsinghua University
Jianlin Lei: Tsinghua University
Yi Wang: China Agricultural University
Guanghui Yang: China Agricultural University

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract The voltage-gated potassium channel AKT1 is responsible for primary K+ uptake in Arabidopsis roots. AKT1 is functionally activated through phosphorylation and negatively regulated by a potassium channel α-subunit AtKC1. However, the molecular basis for the modulation mechanism remains unclear. Here we report the structures of AKT1, phosphorylated-AKT1, a constitutively-active variant, and AKT1-AtKC1 complex. AKT1 is assembled in 2-fold symmetry at the cytoplasmic domain. Such organization appears to sterically hinder the reorientation of C-linkers during ion permeation. Phosphorylated-AKT1 adopts an alternate 4-fold symmetric conformation at cytoplasmic domain, which indicates conformational changes associated with symmetry switch during channel activation. To corroborate this finding, we perform structure-guided mutagenesis to disrupt the dimeric interface and identify a constitutively-active variant Asp379Ala mediates K+ permeation independently of phosphorylation. This variant predominantly adopts a 4-fold symmetric conformation. Furthermore, the AKT1-AtKC1 complex assembles in 2-fold symmetry. Together, our work reveals structural insight into the regulatory mechanism for AKT1.

Date: 2022
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DOI: 10.1038/s41467-022-33420-8

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