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Related Concept Videos

Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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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...
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COP Coated Vesicles00:59

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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...
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Pinching-off of Coated Vesicles01:32

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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...
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Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Assembly of Signaling Complexes01:30

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
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Structure of Cadherins01:25

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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
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Related Experiment Video

Updated: Jun 27, 2025

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

Stéphane Vassilopoulos1, Guillaume Montagnac2

  • 1Sorbonne Université, Inserm U974, Institut de Myologie, Centre de Recherche en Myologie, 75013 Paris, France.

Journal of Cell Science
|April 26, 2024
PubMed
Summary
This summary is machine-generated.

Clathrin, a protein forming honeycomb structures, plays diverse roles beyond intracellular trafficking, including cell adhesion and mitosis. Its structural flexibility enables various functions in mammalian cells.

Keywords:
ClathrinElectron microscopyEndocytosisEndosomePlasma membraneTrans-Golgi network

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Clathrin forms lattice structures on cellular membranes, primarily known for intracellular trafficking.
  • Beyond endocytosis, clathrin participates in non-canonical functions like cell adhesion and mitosis.

Purpose of the Study:

  • To review canonical and non-canonical membrane-associated clathrin assemblies in mammalian cells.
  • To discuss the relationship between clathrin's structural plasticity and its diverse functions.

Main Methods:

  • Review of existing literature and electron microscopy data (thin-section and platinum replica).
  • Analysis of clathrin assemblies in various mammalian cell types.

Main Results:

  • Identified diverse clathrin assembly types, both canonical and non-canonical.
  • Clathrin assemblies are found at the plasma membrane, Golgi, endosomes, and kinetochore k-fibers.
  • Clathrin's structural plasticity underlies its varied roles.

Conclusions:

  • Clathrin exhibits significant functional diversity driven by its structural adaptability.
  • Understanding clathrin assemblies is crucial for comprehending fundamental cellular processes.