该研究组发现了一个序列蛋白磷酸化途径，其中两种不同类型的Raf样蛋白激酶C5-Raf和C7-Raf形成一个异复合体，磷酸化Thr881以激活PM H+-ATP酶。这一调控系统在从苔类植物到被子植物的谱系中高度保守。在拟南芥中，C5-Raf Raf36通过磷酸化多个拟南芥H+-ATP酶（AHAs）来调节植物生长。另外，另一种C5-Raf HT1与c7-Raf CBC1/2一起磷酸化AHA1T881，从而产生光诱导气孔打开的驱动力。他们的发现为理解PM H+-ATP酶在各种生理过程中的激活提供了一个框架，特别是在阐明光诱导气孔打开的完整机制方面。
据悉，质膜质子泵[PM H+-腺苷三磷酸酶（PM H+-ATP酶）]在植物中是必不可少的。C端磷酸化事件调节质子泵活性，如拟南芥AHA1中Thr881的磷酸化。
附：英文原文
Title: Raf-like protein kinase heterocomplexes directly regulate the plant plasma membrane H+-ATPase
Author: Hinano Takase, Aina Nagano, Shota Yamauchi, Yuki Hayashi, Koji Takahashi, Yoshiaki Kamiyama, Kota Yamashita, Sotaro Katagiri, Yangdan Li, Saashia Fuji, Kyoka Tahara, Minoru Noguchi, Yoshiki Kawaguchi, Shunsuke Adachi, Yutaka Kodama, Ryuichi Nishihama, Atsushi Takemiya, Toshinori Kinoshita, Taishi Umezawa
Issue&Volume: 2026-05-14
Abstract: The plasma membrane proton pump [PM H+-adenosine triphosphatase (PM H+-ATPase)] is essential in plants. C-terminal phosphorylation events regulate proton pump activity, such as Thr881 phosphorylation in Arabidopsis AHA1. We discovered a sequential protein phosphorylation pathway in which two distinct types of Raf-like protein kinases, C5-Raf and C7-Raf, form a heterocomplex that phosphorylates Thr881 to activate PM H+-ATPases. This regulatory system is highly conserved across lineages from liverworts to angiosperms. In Arabidopsis, a C5-Raf Raf36 regulates plant growth through the phosphorylation of multiple Arabidopsis H+-ATPases (AHAs). Additionally, another C5-Raf HT1 functions with C7-Rafs CBC1/2 to phosphorylate AHA1T881, thereby generating a driving force for light-induced stomatal opening. Our findings provide a framework for understanding PM H+-ATPase activation in various physiological processes, particularly in elucidating the complete mechanistic understanding of light-induced stomatal opening.
DOI: adx9533
Source: https://www.science.org/doi/10.1126/science.adx9533