Dynamics and environmental responses of PATROL1 in arabidopsis subsidiary cells

Takumi Higaki, Mimi Hashimoto-Sugimoto, Kae Akita, Koh Iba, Seiichiro Hasezawa

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)773-780
Number of pages8
JournalPlant and Cell Physiology
Volume55
Issue number4
DOIs
Publication statusPublished - Jan 1 2014

Fingerprint

Arabidopsis
green fluorescent protein
H-transporting ATP synthase
Green Fluorescent Proteins
guard cells
stomatal movement
Proton-Translocating ATPases
cells
plasma membrane
1-phosphatidylinositol 4-kinase
proton pump
phosphatidylinositol 3-kinase
turgor
Cell Membrane
Phosphatidylinositol 3-Kinase
adenosinetriphosphatase
Proton Pumps
1-Phosphatidylinositol 4-Kinase
Arabidopsis thaliana
ions

All Science Journal Classification (ASJC) codes

  • Physiology
  • Plant Science
  • Cell Biology

Cite this

Dynamics and environmental responses of PATROL1 in arabidopsis subsidiary cells. / Higaki, Takumi; Hashimoto-Sugimoto, Mimi; Akita, Kae; Iba, Koh; Hasezawa, Seiichiro.

In: Plant and Cell Physiology, Vol. 55, No. 4, 01.01.2014, p. 773-780.

Research output: Contribution to journalArticle

Higaki, T, Hashimoto-Sugimoto, M, Akita, K, Iba, K & Hasezawa, S 2014, 'Dynamics and environmental responses of PATROL1 in arabidopsis subsidiary cells', Plant and Cell Physiology, vol. 55, no. 4, pp. 773-780. https://doi.org/10.1093/pcp/pct151
Higaki, Takumi ; Hashimoto-Sugimoto, Mimi ; Akita, Kae ; Iba, Koh ; Hasezawa, Seiichiro. / Dynamics and environmental responses of PATROL1 in arabidopsis subsidiary cells. In: Plant and Cell Physiology. 2014 ; Vol. 55, No. 4. pp. 773-780.
@article{4558dc73682041f78ae509b07dca069e,
title = "Dynamics and environmental responses of PATROL1 in arabidopsis subsidiary cells",
abstract = "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.",
author = "Takumi Higaki and Mimi Hashimoto-Sugimoto and Kae Akita and Koh Iba and Seiichiro Hasezawa",
year = "2014",
month = "1",
day = "1",
doi = "10.1093/pcp/pct151",
language = "English",
volume = "55",
pages = "773--780",
journal = "Plant and Cell Physiology",
issn = "0032-0781",
publisher = "Oxford University Press",
number = "4",

}

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

PY - 2014/1/1

Y1 - 2014/1/1

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.

UR - http://www.scopus.com/inward/record.url?scp=84898875931&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84898875931&partnerID=8YFLogxK

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 -