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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...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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...
Structure of Cadherins01:25

Structure of Cadherins

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 diversity of cadherins...
Intracellular Signaling Affects Focal Adhesions01:17

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...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

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Related Experiment Video

Updated: May 23, 2026

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

Adaptor autoregulation promotes coordinated binding within clathrin coats.

Chao-Wei Hung1, Quyen L Aoh1, Ajit P Joglekar2

  • 1Department of Biology, University of North Carolina Chapel Hill, Chapel Hill, North Carolina 27599.

The Journal of Biological Chemistry
|March 30, 2012
PubMed
Summary
This summary is machine-generated.

Researchers discovered a new autoregulatory motif in the Gga2 clathrin adaptor. This finding explains how clathrin coats assemble correctly for essential membrane traffic.

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

Published on: October 20, 2014

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

Related Experiment Videos

Last Updated: May 23, 2026

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

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

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Membrane traffic facilitates essential protein and lipid exchange between cellular compartments.
  • Clathrin-mediated transport, crucial for cellular responses, involves adaptor proteins linking cargo to clathrin.
  • The precise assembly of clathrin coats, driven by complex adaptor-clathrin interactions, remains incompletely understood.

Purpose of the Study:

  • To investigate the regulatory mechanisms governing clathrin coat assembly.
  • To identify novel interactions and motifs within clathrin adaptors.
  • To elucidate how spatiotemporal control of coat formation is achieved.

Main Methods:

  • Investigated the clathrin adaptor Gga2 and its interactions.
  • Characterized a novel autoregulatory motif within Gga2.
  • Analyzed the synergistic binding of Gga2 to clathrin and the adaptor Ent5.

Main Results:

  • Discovered a new autoregulatory motif in the clathrin adaptor Gga2.
  • Demonstrated that this motif drives synergistic binding of Gga2 to both clathrin and the adaptor Ent5.
  • Showed that this autoregulation impacts the timing and location of Gga2-Ent5 interactions.

Conclusions:

  • The identified autoregulatory motif in Gga2 provides built-in regulation for clathrin coat assembly.
  • Synergistic binding mechanisms are critical for ensuring the correct spatiotemporal formation of clathrin coats.
  • This discovery advances our understanding of the molecular basis of membrane traffic regulation.