ArticleNature communications2023
Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 14 citations in OpenAlex.
- A drought stress-responsive metabolite malate modulates stomatal responses through G-protein-dependent pathway in grapevine and Arabidopsis.Molecular horticulture · 2026Article
- Structural insights into the coordinated regulation of the SLAH family in Arabidopsis thaliana.Nature communications · 2025Article
- OPEN STOMATA 1 activates SLAC1 anion channel primarily through CPK15 in ABA-induced stomatal closure inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Apoplastic metabolomics reveals sugars as mesophyll messengers regulating guard cell ion transport under red light.Nature plants · 2025Article
- ZmGCT1/2 negatively regulate drought tolerance in maize by inhibiting ZmSLAC1 to maintain guard cell turgor.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis for malate-driven, pore lipid-regulated activation of the Arabidopsis vacuolar anion channel ALMT9.Nature communications · 2025Article
- Mechanistic insights into phosphoactivation of SLAC1 in guard cell signaling.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The Potential Role of Genic-SSRs in Driving Ecological Adaptation Diversity inInternational journal of molecular sciences · 2024Article
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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