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 CO 2 assimilation rate, promoting plant growth.
| Original language | English |
|---|---|
| Article number | 3215 |
| Journal | Nature communications |
| Volume | 4 |
| DOIs | |
| Publication status | Published - Aug 15 2013 |
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All Science Journal Classification (ASJC) codes
- Chemistry(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Physics and Astronomy(all)
Cite this
A Munc13-like protein in Arabidopsis mediates H+-ATPase translocation that is essential for stomatal responses. / Hashimoto-Sugimoto, Mimi; Higaki, Takumi; Yaeno, Takashi; Nagami, Ayako; Irie, Mari; Fujimi, Miho; Miyamoto, Megumi; Akita, Kae; Negi, Juntaro; Shirasu, Ken; Hasezawa, Seiichiro; Iba, Koh.
In: Nature communications, Vol. 4, 3215, 15.08.2013.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A Munc13-like protein in Arabidopsis mediates H+-ATPase translocation that is essential for stomatal responses
AU - Hashimoto-Sugimoto, Mimi
AU - Higaki, Takumi
AU - Yaeno, Takashi
AU - Nagami, Ayako
AU - Irie, Mari
AU - Fujimi, Miho
AU - Miyamoto, Megumi
AU - Akita, Kae
AU - Negi, Juntaro
AU - Shirasu, Ken
AU - Hasezawa, Seiichiro
AU - Iba, Koh
PY - 2013/8/15
Y1 - 2013/8/15
N2 - 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 CO 2 assimilation rate, promoting plant growth.
AB - 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 CO 2 assimilation rate, promoting plant growth.
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U2 - 10.1038/ncomms3215
DO - 10.1038/ncomms3215
M3 - Article
C2 - 23896897
AN - SCOPUS:84881356948
VL - 4
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
M1 - 3215
ER -