Raf-like protein kinase heterocomplexes directly regulate the plant plasma membrane H + -ATPase
- 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
2026-05-14
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.