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Related Concept Videos

Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Vesicular Tubular Clusters01:45

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...
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
Clathrin Coated Vesicles01:12

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...
Coat Assembly and GTPases01:33

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...

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Related Experiment Video

Updated: Jun 13, 2026

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

Vesicular traffic: a Rab SANDwich.

Michal Bohdanowicz1, Sergio Grinstein

  • 1Cell Biology Program, Hospital for Sick Children and Institute of Medical Science, University of Toronto, Toronto, Canada.

Current Biology : CB
|April 16, 2010
PubMed
Summary
This summary is machine-generated.

A newly discovered protein complex bridges the gap between Rab5 and Rab7, crucial proteins in phagosome maturation. This finding clarifies the transition mechanism between distinct stages of phagosome development.

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Utilizing pHluorin-tagged Receptors to Monitor Subcellular Localization and Trafficking
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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag

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Related Experiment Videos

Last Updated: Jun 13, 2026

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

Utilizing pHluorin-tagged Receptors to Monitor Subcellular Localization and Trafficking
09:59

Utilizing pHluorin-tagged Receptors to Monitor Subcellular Localization and Trafficking

Published on: March 16, 2017

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
08:55

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag

Published on: December 14, 2017

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Phagosome maturation involves sequential stages marked by small GTPases Rab5 and Rab7.
  • The mechanism connecting these distinct stages has remained largely unknown.

Purpose of the Study:

  • To elucidate the molecular mechanism governing the transition between Rab5- and Rab7-mediated stages of phagosome maturation.

Main Methods:

  • Utilized Caenorhabditis elegans as a model organism.
  • Investigated protein interactions and complex formation.
  • Analyzed the role of newly identified proteins in phagosome trafficking.

Main Results:

  • Identified a novel protein complex that directly links Rab5 and Rab7.
  • Demonstrated the complex's essential role in facilitating the transition from early to late phagosome stages.

Conclusions:

  • The newly identified protein complex is a key regulator of phagosome maturation.
  • This discovery provides a molecular explanation for the sequential connection between Rab5 and Rab7 during phagosome development.