Related Experiment Video
Updated: May 28, 2026

17:14
In vivo and in vitro Studies of Adaptor-clathrin Interaction
Published on: January 26, 2011
Clathrin is required for Scar/Wave-mediated lamellipodium formation
Jérémie J Gautier1, Maria E Lomakina, Lamia Bouslama-Oueghlani
1CNRS UPR3082, Laboratoire d'Enzymologie et Biochimie Structurales, Avenue de la Terrasse, 91198 Gif-sur-Yvette Cedex, France.
Journal of Cell Science
|October 20, 2011
Summary
Clathrin heavy chain (CHC) regulates cell migration by controlling actin network formation. This study reveals CHC
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The Scar/Wave complex (SWC) is crucial for generating lamellipodia via Arp2/3-dependent actin polymerization.
- Identifying novel regulators of SWC activity is essential for understanding cell migration dynamics.
Purpose of the Study:
- To identify new regulators of the Scar/Wave complex (SWC).
- To elucidate the role of Clathrin heavy chain (CHC) in lamellipodium formation and cell migration.
Main Methods:
- Proteomics and functional genomics screen in Drosophila cells.
- Experimental manipulation of Clathrin heavy chain (CHC) localization and expression.
- Analysis of SWC membrane recruitment, protrusion velocity, and cell migration.
Main Results:
- Clathrin heavy chain (CHC) was identified as a protein interacting with the SWC.
- CHC depletion impaired lamellipodium formation, independent of its role in membrane trafficking.
- Altering CHC localization modulated SWC membrane recruitment, affecting protrusion velocity and cell migration.
Conclusions:
- Clathrin heavy chain (CHC) plays a novel role in controlling lamellipodium formation.
- CHC facilitates the recruitment of the SWC to the plasma membrane, thereby regulating cell migration.
Related Concept Videos
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...
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...
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...
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...
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 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...
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...
Some...

