A Munc13-like protein in Arabidopsis mediates H+-ATPase translocation that is essential for stomatal responses
Mimi Hashimoto-Sugimoto,
Takumi Higaki,
Takashi Yaeno,
Ayako Nagami,
Mari Irie,
Miho Fujimi,
Megumi Miyamoto,
Kae Akita,
Juntaro Negi,
Ken Shirasu,
Seiichiro Hasezawa and
Koh Iba ()
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Mimi Hashimoto-Sugimoto: Faculty of Sciences, Kyushu University
Takumi Higaki: Graduate School of Frontier Sciences, The University of Tokyo
Takashi Yaeno: Plant Science Center, RIKEN
Ayako Nagami: Faculty of Sciences, Kyushu University
Mari Irie: Faculty of Sciences, Kyushu University
Miho Fujimi: Faculty of Sciences, Kyushu University
Megumi Miyamoto: Faculty of Sciences, Kyushu University
Kae Akita: Graduate School of Frontier Sciences, The University of Tokyo
Juntaro Negi: Faculty of Sciences, Kyushu University
Ken Shirasu: Plant Science Center, RIKEN
Seiichiro Hasezawa: Graduate School of Frontier Sciences, The University of Tokyo
Koh Iba: Faculty of Sciences, Kyushu University
Nature Communications, 2013, vol. 4, issue 1, 1-9
Abstract:
Abstract Plants control CO2 uptake and water loss by modulating the aperture of stomata located in the epidermis. Stomatal opening is initiated by the activation of H+-ATPases in the guard-cell plasma membrane. In contrast to regulation of H+-ATPase activity, little is known about the translocation of the guard cell H+-ATPase to the plasma membrane. Here we describe the isolation of an Arabidopsis gene, PATROL1, that controls the translocation of a major H+-ATPase, AHA1, to the plasma membrane. PATROL1 encodes a protein with a MUN domain, known to mediate synaptic priming in neuronal exocytosis in animals. Environmental stimuli change the localization of plasma membrane-associated PATROL1 to an intracellular compartment. Plasma membrane localization of AHA1 and stomatal opening require the association of PATROL1 with AHA1. Increased stomatal opening responses in plants overexpressing PATROL1 enhance the CO2 assimilation rate, promoting plant growth.
Date: 2013
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3215
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DOI: 10.1038/ncomms3215
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