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
N1 - Funding Information:
We are grateful to N. Brose and L. Serna for critical reading of the manuscript, and E.M. Jorgensen, J.I. Schroeder and T. Teramoto for comments on the manuscript. We thank T. Sakaguchi for the technical assistance. We also thank R.Y. Tsien for making the mRFP gene available, and the Arabidopsis Biological Resource Center and Cereon Genomics for access to polymorphism information. This research was supported in part by Grants-in-Aid for 21114002 (K.I.), 24114007 (S.H.), 22114505 (S.H), 24228008 (K.S.), 25711017 (T.H.) and 24780046 (T.Y.) from the Ministry of Education, Science and Culture of Japan, and by the Program for Promotion of Basic and Applied Research for Innovations in Bio-Oriented Industry (K.I.), and the Advanced Measurement and Analysis grant from the Japan Science and Technology Agency (S.H.). M.H.-S. is grateful for the financial support from the Fumi Yamamura Memorial Foundation for Female Natural Scientists.
PY - 2013
Y1 - 2013
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 - 2215
ER -