{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["118(18)"],"submitter":["Deng YN"],"pubmed_abstract":["Stomata in leaves regulate gas exchange between the plant and its atmosphere. Various environmental stimuli elicit abscisic acid (ABA); ABA leads to phosphoactivation of slow anion channel 1 (SLAC1); SLAC1 activity reduces turgor pressure in aperture-defining guard cells; and stomatal closure ensues. We used electrophysiology for functional characterizations of Arabidopsis thaliana SLAC1 (AtSLAC1) and cryoelectron microscopy (cryo-EM) for structural analysis of Brachypodium distachyon SLAC1 (BdSLAC1), at 2.97-Å resolution. We identified 14 phosphorylation sites in AtSLAC1 and showed nearly 330-fold channel-activity enhancement with 4 to 6 of these phosphorylated. Seven SLAC1-conserved arginines are poised in BdSLAC1 for regulatory interaction with the N-terminal extension. This BdSLAC1 structure has its pores closed, in a basal state, spring loaded by phenylalanyl residues in high-energy conformations. SLAC1 phosphorylation fine-tunes an equilibrium between basal and activated SLAC1 trimers, thereby controlling the degree of stomatal opening."],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["e2015151118"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8106318"],"repository":["biostudies-literature"],"pubmed_title":["Structure and activity of SLAC1 channels for stomatal signaling in leaves."],"pmcid":["PMC8106318"],"pubmed_authors":["Clarke OB","Qin L","Deng YN","Wang YC","Li F","Su M","Xie Q","Zhen GX","Huang XH","Kashtoh H","Wang Q","Li QY","Hendrickson WA","Zhang CR","Tang LH","Chen YH","Gao HL"],"additional_accession":[]},"is_claimable":false,"name":"Structure and activity of SLAC1 channels for stomatal signaling in leaves.","description":"Stomata in leaves regulate gas exchange between the plant and its atmosphere. Various environmental stimuli elicit abscisic acid (ABA); ABA leads to phosphoactivation of slow anion channel 1 (SLAC1); SLAC1 activity reduces turgor pressure in aperture-defining guard cells; and stomatal closure ensues. We used electrophysiology for functional characterizations of Arabidopsis thaliana SLAC1 (AtSLAC1) and cryoelectron microscopy (cryo-EM) for structural analysis of Brachypodium distachyon SLAC1 (BdSLAC1), at 2.97-Å resolution. We identified 14 phosphorylation sites in AtSLAC1 and showed nearly 330-fold channel-activity enhancement with 4 to 6 of these phosphorylated. Seven SLAC1-conserved arginines are poised in BdSLAC1 for regulatory interaction with the N-terminal extension. This BdSLAC1 structure has its pores closed, in a basal state, spring loaded by phenylalanyl residues in high-energy conformations. SLAC1 phosphorylation fine-tunes an equilibrium between basal and activated SLAC1 trimers, thereby controlling the degree of stomatal opening.","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 May","modification":"2025-04-04T11:00:44.437Z","creation":"2025-04-04T11:00:44.437Z"},"accession":"S-EPMC8106318","cross_references":{"pubmed":["33926963"],"doi":["10.1073/pnas.2015151118"]}}