Asset Details
Do you wish to reserve the book?
Structure of the Arabidopsis guard cell anion channel SLAC1 suggests activation mechanism by phosphorylation
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Structure of the Arabidopsis guard cell anion channel SLAC1 suggests activation mechanism by phosphorylation
Do you wish to request the book?
Structure of the Arabidopsis guard cell anion channel SLAC1 suggests activation mechanism by phosphorylation
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Structure of the Arabidopsis guard cell anion channel SLAC1 suggests activation mechanism by phosphorylation
2022
Overview
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
(
At
SLAC1) in an inactivated, closed state. The cytosolic amino (N)-terminus and carboxyl (C)-terminus of
At
SLAC1 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.
The anion channel SLAC1 controls stomatal closure upon phosphoactivation. Here via structural analysis and electrophysiology, the authors propose an inhibition-release model where phosphorylation causes dissociation of a cytosolic plug from the SLAC1 transmembrane domains to induce conformational change in the pore-forming helices.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 101/58
/ 82/80
/ 82/83
/ 9/74
/ 9/97
/ Abscisic Acid - pharmacology
/ Anions
/ Arabidopsis Proteins - genetics
/ Arabidopsis Proteins - metabolism
/ Closures
/ Domains
/ Helices
/ Humanities and Social Sciences
/ Ion flux
/ Kinases
/ Membrane Proteins - metabolism
/ Plugs
/ Science
/ Stomata
/ Turgor
