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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...
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...
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...
Mechanism of Lamellipodia Formation01:31

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...
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...
Mechanism of Filopodia Formation01:39

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...

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Related Experiment Video

Updated: Jun 28, 2026

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

Dab2 regulates clathrin assembly and cell spreading.

David Chetrit1, Naomi Ziv, Marcelo Ehrlich

  • 1Department of Cell Research and Immunology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.

The Biochemical Journal
|November 13, 2008
PubMed
Summary
This summary is machine-generated.

Disabled 2 (Dab2) protein, a clathrin adaptor, influences cell shape by regulating clathrin assembly dynamics. Dab2

More Related Videos

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

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: Jun 28, 2026

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

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

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:

  • Clathrin-mediated endocytosis is crucial for cellular processes.
  • Endocytic adaptors regulate clathrin assembly at the plasma membrane.
  • Dab2 (disabled 2) is a key adaptor protein involved in endocytosis.

Purpose of the Study:

  • To investigate the role of Dab2 isoforms and mutants in clathrin assembly.
  • To characterize the effect of Dab2 on clathrin-coated pit dynamics.
  • To explore the function of Dab2 in cell spreading and integrin-mediated adhesion.

Main Methods:

  • Utilized GFP (green fluorescent protein) fusion constructs of rat Dab2 isoforms and mutants.
  • Analyzed clathrin assembly size, distribution, and dynamics in COS7 cells.
  • Assessed cell spreading on fibronectin and integrin localization.

Main Results:

  • Overexpression of Dab2 p82 isoform enlarged clathrin assemblies at the plasma membrane.
  • Dab2-clathrin assemblies are dynamic and recruit other endocytic proteins (AP2, epsin).
  • Dab2's ability to induce enlarged assemblies and enhance cell spreading depends on its PTB domain, clathrin/phospholipid binding, and a poly-lysine stretch.

Conclusions:

  • Dab2 plays a significant role in regulating clathrin assembly dynamics.
  • The PTB domain, clathrin/phospholipid binding, and poly-lysine stretch are critical for Dab2 function.
  • Dab2 and clathrin are implicated in integrin-mediated cell spreading and focal adhesion formation.