Raf-like protein kinase heterocomplexes directly regulate the plant plasma membrane H+-ATPase

• 成果类型: Article
• 署名作者: Takase, Hinano; Nagano, Aina; Yamauchi, Shota; Hayashi, Yuki; Takahashi, Koji; Kamiyama, Yoshiaki; Yamashita, Kota; Katagiri, Sotaro; Li, Yangdan; Fuji, Saashia; Tahara, Kyoka; Noguchi, Minoru; Kawaguchi, Yoshiki; Adachi, Shunsuke; Kodama, Yutaka; Nishihama, Ryuichi; Takemiya, Atsushi; Kinoshita, Toshinori; Umezawa, Taishi
• 署名单位: Tokyo University of Agriculture & Technology; Tokyo University of Science; Nagoya University; Nagoya University; Yamaguchi University; Utsunomiya University; Tokyo University of Agriculture & Technology; Tokyo University of Science
• 刊物名称: SCIENCE
• ISSN/ISSBN: 0036-8075; 1095-9203
• DOI: 10.1126/science.adx9533
• 发表日期: 2026-05-14
• 页码: 755-760
• 关键词: PROTON PUMP; arabidopsis-thaliana; light; co2; phosphorylation; activation; EVOLUTION; gene

摘要

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 Thr(881) 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 Thr(881) 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 AHA1(T881), 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.