Arabidopsis G-protein β subunit AGB1 represses abscisic acid signaling via attenuation of the MPK3–VIP1 phosphorylation cascade

• Published in: Journal of experimental botany Vol. 75; no. 5; pp. 1615 - 1632
• Main Authors: Xu, Dongbei, Tang, Wensi, Ma, Yanan, Wang, Xia, Yang, Yanzhi, Wang, Xiaoting, Xie, Lina, Huang, Suo, Qin, Tengfei, Tang, Weilin, Xu, Zhaoshi, Li, Lei, Tang, Yimiao, Chen, Ming, Ma, Youzhi
• Format: Journal Article
• Language: English
• Published: UK Oxford University Press 28-02-2024
• Subjects: Abscisic acid signaling; Arabidopsis; G-protein β subunit; VIP1 transcription factor; MPK3
• ISSN: 0022-0957; 1460-2431
• DOI: 10.1093/jxb/erad464

Abstract
Heterotrimeric G proteins play key roles in cellular processes. Although phenotypic analyses of Arabidopsis Gβ (AGB1) mutants have implicated G proteins in abscisic acid (ABA) signaling, the AGB1-mediated modules involved in ABA responses remain unclear. We found that a partial AGB1 protein was localized to the nucleus where it interacted with ABA-activated VirE2-interacting protein 1 (VIP1) and mitogen-activated protein kinase 3 (MPK3). AGB1 acts as an upstream negative regulator of VIP1 activity by initiating responses to ABA and drought stress, and VIP1 regulates the ABA signaling pathway in an MPK3-dependent manner in Arabidopsis. AGB1 outcompeted VIP1 for interaction with the C-terminus of MPK3, and prevented phosphorylation of VIP1 by MPK3. Importantly, ABA treatment reduced AGB1 expression in the wild type, but increased in vip1 and mpk3 mutants. VIP1 associates with ABA response elements present in the AGB1 promoter, forming a negative feedback regulatory loop. Thus, our study defines a new mechanism for fine-tuning ABA signaling through the interplay between AGB1 and MPK3–VIP1. Furthermore, it suggests a common G protein mechanism to receive and transduce signals from the external environment.
The Arabidopsis G protein β subunit AGB1 interacts with the MPK3–VIP1 module, and acts as a negative regulator of the MPK3–VIP1 phosphorylation cascade to fine-tune ABA signaling.