Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model

Yeongmok Lee, Hyeon Seong Jeong, Seoyeon Jung, Junmo Hwang, Chi Truc Han Le, Sung-Hoon Jun, Eun Jo Du, KyeongJin Kang, Beom-Gi Kim, Hyun-Ho Lim and Sangho Lee ()
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Yeongmok Lee: Sungkyunkwan University
Hyeon Seong Jeong: Neurovascular Unit Research Group, Korea Brain Research Institute
Seoyeon Jung: Sungkyunkwan University
Junmo Hwang: Neurovascular Unit Research Group, Korea Brain Research Institute
Chi Truc Han Le: Sungkyunkwan University
Sung-Hoon Jun: Korea Basic Science Institute
Eun Jo Du: Neurovascular Unit Research Group, Korea Brain Research Institute
KyeongJin Kang: Neurovascular Unit Research Group, Korea Brain Research Institute
Beom-Gi Kim: Metabolic Engineering Division, National Institute of Agricultural Sciences, Rural Development Administration
Hyun-Ho Lim: Neurovascular Unit Research Group, Korea Brain Research Institute
Sangho Lee: Sungkyunkwan University

Nature Communications, 2023, vol. 14, issue 1, 1-16

Abstract: Abstract The anion channel SLAC1 functions as a crucial effector in the ABA signaling, leading to stomata closure. SLAC1 is activated by phosphorylation in its intracellular domains. Both a binding-activation model and an inhibition-release model for activation have been proposed based on only the closed structures of SLAC1, rendering the structure-based activation mechanism controversial. Here we report cryo-EM structures of Arabidopsis SLAC1 WT and its phosphomimetic mutants in open and closed states. Comparison of the open structure with the closed ones reveals the structural basis for opening of the conductance pore. Multiple phosphorylation of an intracellular domain (ICD) causes dissociation of ICD from the transmembrane domain. A conserved, positively-charged sequence motif in the intracellular loop 2 (ICL2) seems to be capable of sensing of the negatively charged phosphorylated ICD. Interactions between ICL2 and ICD drive drastic conformational changes, thereby widening the pore. From our results we propose that SLAC1 operates by a mechanism combining the binding-activation and inhibition-release models.

Date: 2023
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DOI: 10.1038/s41467-023-43193-3

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