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-Structure paper
Title | Structure and activity of SLAC1 channels for stomatal signaling in leaves. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 118, Issue 18, Year 2021 |
Publish date | May 4, 2021 |
Authors | Ya-Nan Deng / Hamdy Kashtoh / Quan Wang / Guang-Xiao Zhen / Qi-Yu Li / Ling-Hui Tang / Hai-Long Gao / Chun-Rui Zhang / Li Qin / Min Su / Fei Li / Xia-He Huang / Ying-Chun Wang / Qi Xie / Oliver B Clarke / Wayne A Hendrickson / Yu-Hang Chen / |
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); ...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 SLAC1 (SLAC1) and cryoelectron microscopy (cryo-EM) for structural analysis of SLAC1 (SLAC1), at 2.97-Å resolution. We identified 14 phosphorylation sites in SLAC1 and showed nearly 330-fold channel-activity enhancement with 4 to 6 of these phosphorylated. Seven SLAC1-conserved arginines are poised in SLAC1 for regulatory interaction with the N-terminal extension. This SLAC1 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. |
External links | Proc Natl Acad Sci U S A / PubMed:33926963 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.97 Å |
Structure data | EMDB-31197, PDB-7en0: |
Chemicals | ChemComp-PLC: ChemComp-SPH: |
Source |
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Keywords | MEMBRANE PROTEIN / anion channel |