Related Experiment Video
Updated: May 23, 2026
12:40
Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
Published on: October 20, 2014
A feedback loop between dynamin and actin recruitment during clathrin-mediated endocytosis
Marcus J Taylor1, Marko Lampe, Christien J Merrifield
1MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Plos Biology
|April 17, 2012
Summary
Dynamin and actin form a feedback loop to drive membrane scission during clathrin-mediated endocytosis. This cooperation ensures efficient cell membrane repair and protein trafficking.
Area of Science:
- Cell Biology
- Molecular Biology
- Biophysics
Background:
- Clathrin-mediated endocytosis (CME) is crucial for cellular processes.
- Membrane scission, the final step in CME, is dynamin-dependent.
- The roles of actin and N-BAR proteins in scission are not fully understood.
Purpose of the Study:
- To investigate the coordination between dynamin, actin, and N-BAR proteins during CME.
- To elucidate the regulatory mechanisms and interdependencies governing protein recruitment in scission.
Main Methods:
- Utilized an optical assay to monitor protein recruitment in real-time.
- Investigated individual clathrin-mediated endocytic scission events.
- Employed latrunculin-B to disrupt actin dynamics.
Main Results:
- Identified a feedback loop between dynamin and actin at scission sites.
- Dynamin GTPase activity modulated the recruitment kinetics of dynamin, actin, and N-BAR proteins.
- Actin disruption reduced scission incidence and dynamin recruitment, abolishing actin and N-BAR recruitment.
Conclusions:
- Dynamin, actin, and N-BAR proteins cooperate for efficient membrane scission.
- Dynamin regulates its own recruitment via actin and N-BAR dynamics.
- Actin acts as a scaffold, concentrating dynamin and N-BAR proteins for scission.
Related Concept Videos
01:32Pinching-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...
01:12Clathrin 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...
01:26Tension Response at Adherens Junctions
The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...
01:31Mechanism 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...
01:17Intracellular 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...
01:39Mechanism 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...