Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

9.8K
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...
9.8K
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

4.3K
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...
4.3K
COP Coated Vesicles00:59

COP Coated Vesicles

18.4K
Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
18.4K
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

9.7K
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...
9.7K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

3.3K
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...
3.3K
Receptor-mediated Endocytosis01:20

Receptor-mediated Endocytosis

10.7K
Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...
10.7K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Systems modelling of mitochondrial dynamics in different exercise regimes.

The Journal of physiology·2026
Same author

A multimodal adaptive optical microscope for in vivo imaging from molecules to organisms.

Nature methods·2026
Same author

Synaptic spine head morphodynamics from graph grammar rules for actin dynamics.

bioRxiv : the preprint server for biology·2026
Same author

A balance between nucleating and elongating actin filaments controls deformation of protein condensates.

Science advances·2026
Same author

Mitochondrial mechanics nucleates axonal jamming and swelling.

ArXiv·2026
Same author

Mitochondrial mechanics nucleates axonal jamming and swelling.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Mar 8, 2026

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
12:40

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy

Published on: October 20, 2014

81.1K

Design principles for robust vesiculation in clathrin-mediated endocytosis.

Julian E Hassinger1, George Oster2, David G Drubin2

  • 1Biophysics Graduate Group, University of California, Berkeley, CA 94720.

Proceedings of the National Academy of Sciences of the United States of America
|January 28, 2017
PubMed
Summary

Cellular membrane budding, essential for cell trafficking, can be hindered by high membrane tension. This study reveals how protein coat properties and actin forces enable robust budding even under tension.

Keywords:
clathrin-mediated endocytosismembrane modelingmembrane tension

More Related Videos

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

15.1K
Patch-Clamp Techniques for Single Endolysosomal Vesicle Analysis
05:47

Patch-Clamp Techniques for Single Endolysosomal Vesicle Analysis

Published on: April 4, 2025

1.3K

Related Experiment Videos

Last Updated: Mar 8, 2026

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
12:40

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy

Published on: October 20, 2014

81.1K
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

15.1K
Patch-Clamp Techniques for Single Endolysosomal Vesicle Analysis
05:47

Patch-Clamp Techniques for Single Endolysosomal Vesicle Analysis

Published on: April 4, 2025

1.3K

Area of Science:

  • Cell Biology
  • Biophysics
  • Mechanobiology

Background:

  • Cellular trafficking relies on membrane budding, a process sensitive to mechanical forces like membrane tension.
  • Clathrin-mediated endocytosis (CME) demonstrates robustness across varying environments, suggesting evolved physical principles.
  • Elevated membrane tension can inhibit protein coat-driven membrane budding.

Purpose of the Study:

  • To investigate the physical principles governing protein coat-mediated membrane budding under varying mechanical conditions.
  • To determine how membrane tension, protein coat properties, and actin polymerization influence bud formation.
  • To identify mechanisms ensuring robust vesiculation despite opposing forces.

Main Methods:

  • Theoretical modeling of membrane mechanics and protein-coat interactions.
  • Systematic investigation of parameters including membrane rigidity, coat curvature, coat area, membrane tension, and actin polymerization force.
  • Analysis of bud formation dynamics under different tension regimes.

Main Results:

  • At low membrane tension, increased coat area or curvature promotes smooth bud formation.
  • High membrane tension flattens the membrane, inhibiting budding.
  • Intermediate tensions exhibit a 'snap-through instability,' transitioning from U-shaped to closed buds.
  • Increased coat rigidity or actin polymerization force can overcome this instability.
  • Combined coat rigidity and actin force ensure robust budding even at high membrane tensions.

Conclusions:

  • Protein coat mechanics and external forces play critical roles in regulating membrane budding.
  • A 'snap-through instability' at intermediate tensions can be modulated by coat properties and actin forces.
  • The interplay between coat rigidity and actin polymerization enables robust cellular vesicle formation under diverse mechanical stresses.