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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...
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...
COP Coated Vesicles00:59

COP Coated Vesicles

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 different...
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
Transport Across the Golgi01:26

Transport Across the Golgi

While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...

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Related Experiment Video

Updated: Jun 21, 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

Integrating Lateral Super-Resolution and Axial Progression Reveals Distinct Clathrin Pit Formation Pathways.

Cristopher Thompson1, Aritra Mondal2, Gregory Lafyatis1

  • 1Department of Physics, The Ohio State University, Columbus, Ohio, USA.

Traffic (Copenhagen, Denmark)
|June 20, 2026
PubMed
Summary
This summary is machine-generated.

We developed variable-angle total internal reflection fluorescence structured illumination microscopy (vaTIRF-SIM) to visualize clathrin coat organization and movement during live-cell endocytosis. This new method reveals how clathrin coats grow and move in 3D, advancing our understanding of vesicle formation.

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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

Label-Retention Expansion Microscopy (LR-ExM) Enables Super-Resolution Imaging and High-Efficiency Labeling
07:44

Label-Retention Expansion Microscopy (LR-ExM) Enables Super-Resolution Imaging and High-Efficiency Labeling

Published on: October 11, 2022

Related Experiment Videos

Last Updated: Jun 21, 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

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

Label-Retention Expansion Microscopy (LR-ExM) Enables Super-Resolution Imaging and High-Efficiency Labeling
07:44

Label-Retention Expansion Microscopy (LR-ExM) Enables Super-Resolution Imaging and High-Efficiency Labeling

Published on: October 11, 2022

Area of Science:

  • Cell Biology
  • Biophysics
  • Microscopy

Background:

  • Clathrin-mediated endocytosis (CME) is crucial for vesicle formation at the plasma membrane.
  • Existing live-cell imaging methods struggle to link clathrin coat nanoscale organization with 3D dynamics.
  • Static structural methods and lower-resolution live-cell techniques limit real-time understanding of CME progression.

Purpose of the Study:

  • To develop a live-cell imaging technique combining super-resolution lateral organization with axial sensitivity.
  • To visualize the real-time, three-dimensional progression of clathrin coats during CME.
  • To investigate the relationship between clathrin coat nanoscale structure and its dynamic movement.

Main Methods:

  • Introduction of variable-angle total internal reflection fluorescence structured illumination microscopy (vaTIRF-SIM).
  • Integration of TIRF-SIM with controlled variation of evanescent field penetration depth.
  • Application to genome-edited SUM-159 cells expressing AP2-EGFP.

Main Results:

  • vaTIRF-SIM enables simultaneous visualization of clathrin coat architecture and axial displacement with high spatiotemporal resolution.
  • Coordinated lateral growth and progressive axial advancement of de novo clathrin-coated pits were observed.
  • Two distinct endocytic behaviors at clathrin plaques were identified: peripheral and rapid subdomain internalization.

Conclusions:

  • vaTIRF-SIM provides the first real-time coupling of nanoscale clathrin coat organization with axial progression during CME.
  • The findings reveal dynamic curvature generation and distinct endocytic pathways associated with clathrin plaques.
  • This technique offers new insights into the mechanics of vesicle formation in living cells.