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Updated: Aug 8, 2026
10:19
Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin
Published on: January 24, 2025
Rab10 Promotes Atlastin-Mediated Endoplasmic Reticulum Membrane Fusion
Minseok Kim1, Kongmin Na1, Hyeonji Kim1
1Department of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, South Korea.
Summary
Rab10 protein enhances endoplasmic reticulum (ER) membrane fusion mediated by atlastin (ATL) GTPases. This study reveals a novel interaction between Rab and dynamin-like GTPases in regulating organelle dynamics.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Intracellular membrane fusion relies on two main GTPase classes: dynamin-like GTPases for organelle fusion and Rab GTPases for vesicle tethering.
- These GTPase classes have not been previously linked to the same fusion event.
Purpose of the Study:
- To investigate the potential role of Rab GTPases in atlastin (ATL)-mediated endoplasmic reticulum (ER) membrane fusion.
- To uncover novel regulatory mechanisms in organelle dynamics.
Main Methods:
- Investigated the physical interaction and co-localization of Rab10 and atlastin 2 (ATL2) in ER membranes.
- Assessed the impact of anti-Rab10 antibodies and Rab10 knockout on ATL2-driven ER microsome fusion.
- Examined the effect of Rab10 on the fusion of ATL2-containing liposomes.
Main Results:
- Rab10 physically interacted with and co-localized with ATL2 at ER three-way junctions.
- ER membrane fusion driven by ATL2 was inhibited by anti-Rab10 antibodies and reduced in Rab10 knockout cells.
- Co-reconstitution with Rab10 significantly enhanced ATL2-mediated liposome fusion.
Conclusions:
- Rab10 promotes ER membrane fusion mediated by the dynamin-like GTPase atlastin.
- Demonstrated crosstalk between dynamin-like and Rab GTPases in ATL-mediated ER fusion.
- Identified a novel regulatory mechanism for organelle dynamics involving Rab10 and ATL GTPases.
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