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Updated: May 2, 2026

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
Published on: March 9, 2012
C-terminal S-acylation governs membrane distribution, interaction dynamics and function of a plant Rho GTPase
Amir Akerman1, Orit Gutman2, Keren E Shapira2
1School of Plant Sciences and Food Security, Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
This study reveals that type-II Rho of Plants (ROPs) are S-acylated in vivo, a modification crucial for regulating plant cell polarity. This finding highlights a key difference between type-I and type-II ROPs.
Area of Science:
- Plant molecular biology
- Cell signaling
- Lipid biochemistry
Background:
- Rho of Plants (ROPs) are plant-specific Rho GTPases regulating cellular processes.
- ROPs are classified as type I or type II based on C-terminal motifs.
- In vivo evidence for type-II ROP S-acylation and function was limited.
Purpose of the Study:
- Investigate membrane association, lipid modifications, and function of Arabidopsis type-II ROP, ROP10.
- Provide in vivo evidence for S-acylation of type-II ROPs.
- Clarify the role of ROP10 in plant cell polarity.
Main Methods:
- Confocal microscopy
- Biochemical fractionation
- Fluorescence recovery after photobleaching (FRAP)
- Gas chromatography-mass spectrometry
Main Results:
- Wild-type ROP10 membrane association is activation- and Cys199/205-dependent, with Cys160 stabilizing it.
- The constitutively active rop10CA mutant showed reduced membrane affinity compared to type-I ROPs.
- Gas chromatography-mass spectrometry confirmed ROP10 S-acylation with palmitic and stearic acids.
- ROP10 Cys160 is essential for polarity control, as rop10C160S mutation abolished polarity disruption.
Conclusions:
- This study provides the first in vivo evidence for S-acylation of type-II ROPs.
- ROP10 S-acylation is critical for regulating plant cell polarity.
- Type-II ROPs diverge from type-I ROPs via distinct plasma membrane subdomain partitioning.
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