Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Clathrin Coated Vesicles

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 Vesicles

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...

Receptor-mediated Endocytosis

Receptor-mediated Endocytosis

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...

Receptor-mediated Endocytosis

Receptor-mediated Endocytosis

Receptor-Mediated Endocytosis

Receptor-Mediated Endocytosis

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...

Intracellular Signaling Affects Focal Adhesions

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...

You might also read

Related Articles

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

Sort by

Same author

FCHO controls AP2's initiating role in endocytosis through a PtdIns(4,5)P<sub>2</sub>-dependent switch.

Science advances·2022

Same author

Atg27p co-fractionates with clathrin-coated vesicles in budding yeast.

microPublication biology·2021

Same author

Atg27p localization is clathrin- and Ent3p/5p-dependent.

microPublication biology·2021

Same author

Ernst Joachim Ungewickell: 1950-2020.

The Journal of cell biology·2020

Same author

A nanobody-based molecular toolkit provides new mechanistic insight into clathrin-coat initiation.

eLife·2019

Same author

Identification of Suppressor of Clathrin Deficiency-1 (<i>SCD1</i>) and Its Connection to Clathrin-Mediated Endocytosis in <i>Saccharomyces cerevisiae</i>.

G3 (Bethesda, Md.)·2019

Search research articles

Related Experiment Video

Updated: May 25, 2026

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

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

Published on: October 20, 2014

Getting in touch with the clathrin terminal domain.

Sandra K Lemmon¹, Linton M Traub

¹Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, FL 33101, USA. slemmon@med.miami.edu

Traffic (Copenhagen, Denmark)

|January 14, 2012

Summary

The N-terminal domain (TD) of clathrin heavy chain acts as a key protein interaction site. Chemical inhibitors block endocytosis by targeting one TD surface, despite functional redundancy.

More Related Videos

In vivo and in vitro Studies of Adaptor-clathrin Interaction

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

Bimolecular Fluorescence Complementation

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

Related Experiment Videos

Last Updated: May 25, 2026

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

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

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

Bimolecular Fluorescence Complementation

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

Area of Science:

Cell Biology
Structural Biology
Biochemistry

Background:

The N-terminal domain (TD) of clathrin heavy chain forms a seven-bladed β-propeller.
This TD is a critical protein-protein interaction hub, particularly at the membrane-proximal inner coat layer.
Interaction with the TD involves short motifs from intrinsically disordered segments of coat components.

Purpose of the Study:

To delineate the interaction surfaces on the TD β-propeller.
To understand the molecular basis of inhibition by chemical compounds like 'pitstop' inhibitors.
To investigate the functional redundancy of TD interaction sites in vivo.

Main Methods:

Structural analysis of the clathrin heavy chain N-terminal domain.
Identification and mapping of protein-protein interaction sites.
Biochemical assays to study inhibitor binding and functional effects.

Main Results:

Four distinct interaction surfaces on the TD β-propeller have been identified.
A large variation exists in the TD-binding motifs recognized by these surfaces.
Functional redundancy of TD interaction sites was observed in vivo.

Conclusions:

The TD β-propeller serves as a major hub for protein interactions in the clathrin coat.
'Pitstop' inhibitors block clathrin-mediated endocytosis by engaging a single TD interaction surface.
The mechanism of potent inhibition despite targeting only one surface warrants further investigation into functional redundancy and allosteric effects.