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Related Concept Videos

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...
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...
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
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...
Pinching-off of Coated Vesicles01:32

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...
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...

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Related Experiment Video

Updated: May 9, 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

Structural disorder provides increased adaptability for vesicle trafficking pathways.

Natalia Pietrosemoli1, Rita Pancsa, Peter Tompa

  • 1National Centre for Biotechnology (CNB-CSIC), Madrid, Spain ; Department of Bioengineering, Rice University, Houston, Texas, USA.

Plos Computational Biology
|July 23, 2013
PubMed
Summary
This summary is machine-generated.

Vesicle trafficking pathways, including clathrin, COPI, and COPII, show conserved structural disorder in yeast and humans. The clathrin system

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Super-resolution Imaging of Neuronal Dense-core Vesicles
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Super-resolution Imaging of Neuronal Dense-core Vesicles

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In vivo and in vitro Studies of Adaptor-clathrin Interaction
17:14

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

Related Experiment Videos

Last Updated: May 9, 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

Super-resolution Imaging of Neuronal Dense-core Vesicles
09:30

Super-resolution Imaging of Neuronal Dense-core Vesicles

Published on: July 2, 2014

In vivo and in vitro Studies of Adaptor-clathrin Interaction
17:14

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

Area of Science:

  • Cell Biology
  • Biochemistry
  • Evolutionary Biology

Background:

  • Vesicle trafficking is crucial for cellular communication, involving clathrin, COPI, and COPII routes.
  • These routes, while sharing basic organization, differ in molecular machinery, function, and evolution.
  • Understanding these differences is key to deciphering cellular processes.

Purpose of the Study:

  • To analyze the structural disorder of protein groups in human and yeast vesicle trafficking routes.
  • To investigate the correlation between structural disorder, protein multi-functionality (moonlighting), and evolutionary adaptability.
  • To compare the disorder content and adaptability of the clathrin, COPI, and COPII systems.

Main Methods:

  • Comparative analysis of protein structural disorder in human and yeast.
  • Assessment of protein multi-functionality (moonlighting) and its link to disorder.
  • Examination of tissue-specific gene expression and exon characteristics related to disorder.

Main Results:

  • Overall protein disorder is conserved between yeast and human vesicle trafficking systems.
  • The clathrin system exhibits significantly higher disorder (~23%) compared to COPI (~9%) and COPII (~8%).
  • Higher disorder in clathrin correlates with increased plasticity, adaptability, and moonlighting, particularly in clathrin adaptors.

Conclusions:

  • Structural disorder is fundamentally important across vesicle trafficking routes.
  • The elevated disorder in the clathrin system underpins its greater evolutionary adaptability and plasticity.
  • Disordered protein segments in tissue-specific clathrin exons contribute to functional diversification.