National Natural Science Foundation of China (NSFC)
31900885
China
National Natural Science Foundation of China (NSFC)
31870732
China
Other government
2008085MC90
China
Other government
2008085J15
China
Other government
YD9100002004
China
Citation
Journal: Nat Commun / Year: 2022 Title: Structure of the Arabidopsis guard cell anion channel SLAC1 suggests activation mechanism by phosphorylation. Authors: Yawen Li / Yinan Ding / Lili Qu / Xinru Li / Qinxuan Lai / Pingxia Zhao / Yongxiang Gao / Chengbin Xiang / Chunlei Cang / Xin Liu / Linfeng Sun / Abstract: Stomata play a critical role in the regulation of gas exchange and photosynthesis in plants. Stomatal closure participates in multiple stress responses, and is regulated by a complex network ...Stomata play a critical role in the regulation of gas exchange and photosynthesis in plants. Stomatal closure participates in multiple stress responses, and is regulated by a complex network including abscisic acid (ABA) signaling and ion-flux-induced turgor changes. The slow-type anion channel SLAC1 has been identified to be a central controller of stomatal closure and phosphoactivated by several kinases. Here, we report the structure of SLAC1 in Arabidopsis thaliana (AtSLAC1) in an inactivated, closed state. The cytosolic amino (N)-terminus and carboxyl (C)-terminus of AtSLAC1 are partially resolved and form a plug-like structure which packs against the transmembrane domain (TMD). Breaking the interactions between the cytosolic plug and transmembrane domain triggers channel activation. An inhibition-release model is proposed for SLAC1 activation by phosphorylation that the cytosolic plug dissociates from the transmembrane domain upon phosphorylation, and induces conformational changes to open the pore. These findings facilitate our understanding of the regulation of SLAC1 activity and stomatal aperture in plants.
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