The Arabidopsis heterotrimeric G protein α subunit binds to and inhibits the inward rectifying potassium channel KAT1

Copyright © 2024 Elsevier B.V. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant science : an international journal of experimental plant biology. - 1985. - 352(2024) vom: 20. Dez., Seite 112363
1. Verfasser: Guo, Jiang-Fan (VerfasserIn)
Weitere Verfasser: Zhou, Hui, Hu, Zhuo-Ran, Yang, Ya-Lan, Wang, Wen-Bin, Zhang, Yan-Ru, Li, Xue, Mulati, Nuerkaimaier, Li, Ying-Xin, Wu, Lu, Long, Yu, He, Jun-Min
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2024
Zugriff auf das übergeordnete Werk:Plant science : an international journal of experimental plant biology
Schlagworte:Journal Article Gα subunit heterotrimer G proteins interaction inward-rectifying K(+) channels potassium channel in Arabidopsis thaliana 1 transmembrane domains
Beschreibung
Zusammenfassung:Copyright © 2024 Elsevier B.V. All rights reserved.
In animal cells, Gα subunit of the heterotrimeric G proteins can bind to both the N-terminal and C-terminal domains of G-protein-activated inwardly rectifying K+ channels (GIRKs) to inhibit their activities. In Arabidopsis guard cells, the Gα subunit GPA1 mediates multiple stimuli-regulated stomatal movements via inhibiting guard cell inward-rectifying K+ (K+in) current, but it remains unclear whether GPA1 directly interacts with and inhibits the activities of K+in channels. Here, we found that GPA1 interacted with the transmembrane domain rather than the intracellular domain of the Shaker family K+in channel KAT1. Two-Electrode Voltage-Clamp experiments in Xenopus oocytes demonstrated that GPA1 significantly inhibited KAT1 channel activity. However, GPA1 could not inhibit the assembly of KAT1 as well as KAT2 as homo- and hetero-tetramers and alter the subcellular localization and protein stability of these channels. In conclusion, these findings reveal a novel regulatory mechanism for Gα inhibition of the Shaker family K+in channel KAT1 via binding to its channel transmembrane domains but without affecting its subcellular localization, protein stability and the formation of functional homo- and hetero-tetramers. This suggests that in both animal and plant cells, Gα can regulate K+in channels through physical interaction, albeit with differing mechanisms of interaction and regulation
Beschreibung:Date Revised 28.12.2024
published: Print-Electronic
Citation Status Publisher
ISSN:1873-2259
DOI:10.1016/j.plantsci.2024.112363