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Updated: Nov 10, 2025

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
Published on: March 9, 2012
Arf1 orchestrates Rab GTPase conversion at the trans-Golgi network
Laura L Thomas1, Carolyn M Highland1, J Christopher Fromme1
1Department of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853.
Rab GTPases organize membrane trafficking and organelle identity. Arf1 GTPase regulates Rab conversion at the trans-Golgi network by recruiting TRAPPII and Gyp1, ensuring distinct Rab domains.
Area of Science:
- Cell Biology
- Molecular Biology
- Membrane Trafficking
Background:
- Rab GTPases are crucial for membrane trafficking and maintaining organelle identity.
- The yeast Golgi complex exhibits distinct Rab domains, with Ypt1/Rab1 and Ypt6/Rab6 at early/medial Golgi, transitioning to Ypt31/32/Rab11 at the late Golgi/trans-Golgi network (TGN).
- Previous models proposed GTPase-activating protein (GAP) cascades, involving Ypt31/32 recruiting Gyp1 and Gyp6, to explain this Rab conversion.
Purpose of the Study:
- To investigate additional regulatory mechanisms governing Rab transition at the TGN.
- To elucidate the role of the TRAPPII complex and Arf1 GTPase in Rab inactivation at the TGN.
Main Methods:
- Experimental validation of the TRAPPII complex's role in Ypt6 inactivation.
- Investigation of Arf1 GTPase's function in recruiting Gyp1 for Ypt1 inactivation at the TGN.
Main Results:
- Confirmed the TRAPPII complex as a key regulator of Ypt6 inactivation.
- Uncovered a novel role for Arf1 GTPase in recruiting Gyp1 to inactivate Ypt1 at the TGN.
- Demonstrated that Arf1 acts as a master regulator of Rab conversion by recruiting TRAPPII and Gyp1.
Conclusions:
- Rab transition at the TGN involves complex regulatory layers beyond previously known GAP cascades.
- Arf1 GTPase is a central coordinator of Rab conversion, essential for maintaining Golgi compartment identity.
- These findings provide new insights into the precise control of membrane trafficking and organelle organization.
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