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Updated: Jun 20, 2026

Cellular Redox Profiling Using High-content Microscopy

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Published on: May 14, 2017

Intracellular ROS: What Does it Do There?

Yehoram Leshem¹, Alex Levine

¹Department of Plant and Environmental Sciences; The Hebrew University of Jerusalem; Jerusalem, Israel.

Plant Signaling & Behavior

|August 26, 2009

Summary

Salt stress triggers reactive oxygen species (ROS) within endosomes, delivered via vacuolar vesicle trafficking to the tonoplast. This leads to oxidative gating of water channels, reducing root hydraulic conductivity.

Keywords:

TIP VAMP7C intracellular ROS salt stress v SNARE vacuolar trafficking

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Area of Science:

Plant cell biology
Plant physiology
Molecular plant science

Background:

Intracellular localization of reactive oxygen species (ROS) is crucial for understanding cellular responses to environmental stimuli.
Salt stress impacts plant water relations, but the underlying molecular mechanisms require further elucidation.

Purpose of the Study:

To investigate the intracellular localization and role of reactive oxygen species (ROS) during salt stress in Arabidopsis root cells.
To elucidate the mechanism by which ROS signaling influences root hydraulic conductivity under salt stress.

Main Methods:

Tracking intracellular ROS localization using fluorescence microscopy.
Analyzing vacuolar vesicle trafficking pathways.
Assessing tonoplast aquaporin activity and root hydraulic conductivity.

Main Results:

NaCl-induced ROS were localized within endosomes during vacuolar vesicle trafficking to the tonoplast.
ROS delivery to the tonoplast resulted in oxidative gating of TIPs water channels.
Closure of tonoplast aquaporins correlated with reduced root hydraulic conductivity.

Conclusions:

Intracellular ROS, compartmentalized in endosomes, are delivered to the tonoplast via vesicle trafficking, mediating a novel signaling pathway in salt-stressed Arabidopsis roots.
This ROS signaling pathway contributes to the observed reduction in root hydraulic conductivity during salt stress by regulating aquaporin activity.