Raf-like protein kinase heterocomplexes directly regulate the plant plasma membrane H(+)-ATPase
Summary
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 l
Content
# Raf-like protein kinase heterocomplexes directly regulate the plant plasma membrane H(+)-ATPase
*Published: 2026 May 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 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: 10.1126/science.adx9533