Related Experiment Video
Updated: May 11, 2026

08:55
Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
Published on: December 29, 2017
GEF-H1: orchestrating the interplay between cytoskeleton and vesicle trafficking
Ritu Pathak1, Celine Dermardirossian1
1Departments of Immunology and Microbial Science; The Scripps Research Institute; La Jolla, CA USA.
Small Gtpases
|May 8, 2013
Summary
RhoA and GEF-H1 regulate vesicle trafficking by controlling the exocyst complex. This mechanism links RalA signaling to cytoskeletal coordination during cell division and migration.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Vesicle trafficking is essential for cellular functions like division, migration, and secretion.
- Rho GTPases are key regulators of the actin cytoskeleton, but their role in vesicle trafficking is not fully understood.
- The exocyst complex is critical for tethering vesicles to the plasma membrane.
Purpose of the Study:
- To elucidate the molecular mechanism by which RhoA regulates membrane trafficking.
- To investigate the role of GEF-H1 in RhoA-mediated vesicle transport.
- To understand how RalA signaling influences exocyst complex assembly and exocytosis.
Main Methods:
- Investigated RhoA regulation of the exocyst complex.
- Examined the function of GEF-H1 in endocytic and exocytic vesicle trafficking.
- Analyzed RhoA activation by RalA GTPase and its impact on exocytosis.
Main Results:
- GEF-H1 activates RhoA in response to RalA GTPase.
- Activated RhoA regulates the localization and assembly of exocyst components.
- This pathway is involved in both endocytic and exocytic vesicle trafficking.
- A mechanism for RhoA activation during vesicle trafficking was defined.
Conclusions:
- RhoA, activated by GEF-H1 and RalA, plays a critical role in vesicle trafficking.
- This study provides a framework for understanding RhoA/GEF-H1's role in coordinating cytoskeleton dynamics and vesicle transport.
- The findings offer insights into cell division and migration processes.
Related Concept Videos
Coat Assembly and GTPases
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Vesicular Tubular Clusters
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
With the help of motor proteins such...
The Movement of Organelles and Vesicles
In eukaryotic cells, cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
Pinching-off of Coated Vesicles
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
Cytoskeletal Coordination in Cell Migration
A migrating cell changes its shape during the cyclic events of attachment and detachment from the substratum and repositions the cell organelles correspondingly. These complex events are orchestrated by the dynamic cytoskeletal network comprising actin filaments, intermediate filaments, and microtubules. Cytoskeletal crosstalk — the direct and indirect communication between the different components — is crucial for this coordination. Direct communication involves various linker proteins that...
Clathrin Coated Vesicles
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...

