Structural insights into the coordinated regulation of the SLAH family in Arabidopsis thaliana

S-type anion channel homologs (SLAH) are widely expressed in various plant tissues and play a key role in anion transport, which is crucial for plant adaptation to both biotic and abiotic stresses. In this study, we employ cryo-electron microscopy (cryo-EM) to analyze four SLAH channel complexes from Arabidopsis thaliana: the homotrimeric SLAH3 channel, the 2SLAH1 + SLAH3+tRNA complex, the 1SLAH1 + 2SLAH3 complex, and the 3SLAH1+tRNA complex. Critically, our studies reveal that tRNA directly binds to and occupies the intracellular entrance of the SLAH1 homotrimer and the 2SLAH1 + SLAH3 heterocomplex. Electrophysiological experiments confirm tRNA's role as a potent inhibitory regulatory subunit: RNase-mediated tRNA degradation robustly activates SLAH1 currents, while targeted mutagenesis of SLAH1 tRNA-interacting residues phenocopy this activation and enhanced ABA-induced stomatal closure. Combining with structural biology, electrophysiology, and biochemistry, we comprehensively examine the key residues in SLAH1 and SLAH3 that are responsible for the anion permeation. This mechanistic advancement provides a deeper understanding of the molecular basis for plant stress tolerance and identifies specific molecular targets for future engineering crops.

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Publication Details

Journal
Nature Communications
Published
2025-12-17
DOI
https://doi.org/10.1038/s41467-025-67283-6
Primary Topic
Nanopore and Nanochannel Transport Studies
Type
article
Field-Weighted Citation Impact
0.00

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article

Structural insights into the coordinated regulation of the SLAH family in Arabidopsis thaliana

Xueying Huang, Jianping Xie, Zhilin Hao, Jiayi Fan et al.
Nature Communications
Nanopore and Nanochannel Transport Studies
article

Structural insights into the coordinated regulation of the SLAH family in Arabidopsis thaliana

Xueying Huang, Jianping Xie, Zhilin Hao, Jiayi Fan, Tiancong Qi, Kun Cui, Nong Xiao, Sensen Zhang, Botong Liu, Yingcai Song, Maofei Chen, Maojun Yang, Ruochong Li, Kaiwen Yang, Tao Liu, Yujie Li, Chang Liu, Zhiqiang Liu, Xiaojuan Wang, Di Wu, Jian Yin, Jingbo Yi, Jian Mao, Xudong Chen, Boya Qi
article en

Abstract

S-type anion channel homologs (SLAH) are widely expressed in various plant tissues and play a key role in anion transport, which is crucial for plant adaptation to both biotic and abiotic stresses. In this study, we employ cryo-electron microscopy (cryo-EM) to analyze four SLAH channel complexes from Arabidopsis thaliana: the homotrimeric SLAH3 channel, the 2SLAH1 + SLAH3+tRNA complex, the 1SLAH1 + 2SLAH3 complex, and the 3SLAH1+tRNA complex. Critically, our studies reveal that tRNA directly binds to and occupies the intracellular entrance of the SLAH1 homotrimer and the 2SLAH1 + SLAH3 heterocomplex. Electrophysiological experiments confirm tRNA's role as a potent inhibitory regulatory subunit: RNase-mediated tRNA degradation robustly activates SLAH1 currents, while targeted mutagenesis of SLAH1 tRNA-interacting residues phenocopy this activation and enhanced ABA-induced stomatal closure. Combining with structural biology, electrophysiology, and biochemistry, we comprehensively examine the key residues in SLAH1 and SLAH3 that are responsible for the anion permeation. This mechanistic advancement provides a deeper understanding of the molecular basis for plant stress tolerance and identifies specific molecular targets for future engineering crops.

Nature CommunicationsVol. 17(1)
Beijing Institute of Petrochemical Technology (CN), Shanghai Jiao Tong University (CN), Southern University of Science and Technology (CN), Ministry of Education (KR), Beijing Children’s Hospital (CN), Obstetrics and Gynecology Hospital of Fudan University (CN), Shanghai First Maternity and Infant Hospital (CN), Center for Life Sciences (CN), Beijing Academy of Science and Technology (CN), Tsinghua University (CN)
Natural Science Foundation of Shanghai, National Natural Science Foundation of China, Science and Technology Commission of Shanghai Municipality, Tsinghua University, Program of Shanghai Academic Research Leader
Openalex Percentile: Top 60%
Nanopore and Nanochannel Transport Studies
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