TY - JOUR
T1 - Dynamics and environmental responses of PATROL1 in arabidopsis subsidiary cells
AU - Higaki, Takumi
AU - Hashimoto-Sugimoto, Mimi
AU - Akita, Kae
AU - Iba, Koh
AU - Hasezawa, Seiichiro
N1 - Funding Information:
This work was supported by the Ministry of Education, Science and Culture of Japan [Grants-in-Aid to T.H. (25711017), K.I. (21114002) and S.H. (24114007, 22114505 and 25291056)]; the Program for Promotion of Basic and Applied Research for Innovations in Bio-Oriented Industry [Grants-in-Aid to K.I.]; the Advanced Measurement and Analysis grant from the Japan Science and Technology Agency [Grants-in-Aid to S.H.]; the Fumi Yamamura Memorial Foundation for Female Natural Scientists, Japan [financial support to M.H.-S.] .
PY - 2014/4
Y1 - 2014/4
N2 - The Arabidopsis stomatal complex is composed of a pair of guard cells and surrounding anisocytic subsidiary cells. Subsidiary cells are thought to function as a supplier and receiver of bulk water and ions, and to assist turgor-driven stomatal movement, but the molecular mechanisms are largely unknown. In this work, we studied the dynamic behavior and environmental responses of PATROL1, which has been identified as a translocation factor of the plasma membrane proton pump ATPase (PM H+-ATPase) AHA1 in guard cells and subsidiary cells in Arabidopsis thaliana. Variable-angle epifluorescence microscopic observation revealed that green fluorescent protein (GFP)-PATROL1 localized on dot-like compartments that resided on plasma membranes for several seconds. The GFP-PATROL1-labeled dots were sensitive to phosphatidylinositol 4-kinase inhibitors but not to a phosphatidylinositol 3-kinase inhibitor. GFP-PATROL1 and red fluorescent protein (RFP)-AHA1 co-localized in hyperosmotic conditions, and a mutation of PATROL1 resulted in an increase in GFP-AHA1 internalization, suggesting a role in the translocation of PM H+-ATPase in subsidiary cells. Interestingly, subsidiary cells showed changes in localization of GFP-PATROL1 in response to environmental stimuli that were opposite to those in guard cells. Our observations suggested that PATROL1 may contribute to stomatal movement by translocations of PM H +-ATPase in subsidiary cells.
AB - The Arabidopsis stomatal complex is composed of a pair of guard cells and surrounding anisocytic subsidiary cells. Subsidiary cells are thought to function as a supplier and receiver of bulk water and ions, and to assist turgor-driven stomatal movement, but the molecular mechanisms are largely unknown. In this work, we studied the dynamic behavior and environmental responses of PATROL1, which has been identified as a translocation factor of the plasma membrane proton pump ATPase (PM H+-ATPase) AHA1 in guard cells and subsidiary cells in Arabidopsis thaliana. Variable-angle epifluorescence microscopic observation revealed that green fluorescent protein (GFP)-PATROL1 localized on dot-like compartments that resided on plasma membranes for several seconds. The GFP-PATROL1-labeled dots were sensitive to phosphatidylinositol 4-kinase inhibitors but not to a phosphatidylinositol 3-kinase inhibitor. GFP-PATROL1 and red fluorescent protein (RFP)-AHA1 co-localized in hyperosmotic conditions, and a mutation of PATROL1 resulted in an increase in GFP-AHA1 internalization, suggesting a role in the translocation of PM H+-ATPase in subsidiary cells. Interestingly, subsidiary cells showed changes in localization of GFP-PATROL1 in response to environmental stimuli that were opposite to those in guard cells. Our observations suggested that PATROL1 may contribute to stomatal movement by translocations of PM H +-ATPase in subsidiary cells.
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U2 - 10.1093/pcp/pct151
DO - 10.1093/pcp/pct151
M3 - Article
C2 - 24163289
AN - SCOPUS:84898875931
VL - 55
SP - 773
EP - 780
JO - Plant and Cell Physiology
JF - Plant and Cell Physiology
SN - 0032-0781
IS - 4
ER -