Clathrin-coated Pits
Clathrin-coated Pits - Related Videos
01:12
Clathrin Coated Vesicles
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2023
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...
04:46
Resorption Pit Assay: An In Vitro Technique to Quantify Calcium Resorption Activity of Mature Osteoclasts using Calcium Phosphate-Coated Culture Plates
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2025
In this video, we describe an in vitro osteoclastic resorption assay on calcium phosphate-coated cell culture plates cultured with human peripheral blood mononuclear cell-derived osteoclasts. The osteoclasts form a characteristic actin ring on the calcium phosphate-coated matrix of the cell culture plate and degrade the matrix within the actin ring region to release calcium and phosphate ions, resulting in the formation of distinct resorption pits within the degraded matrix.
17:14
In vivo and in vitro Studies of Adaptor-clathrin Interaction
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Cited by 8 •
2011
Clathrin-mediated endocytosis depends on adaptor proteins that coordinate cargo selection and clathrin coat assembly. Here we describe procedures to study adaptor-clathrin physical interaction and live cell imaging approaches using as a model the yeast endocytic adaptor protein Sla1p.
13:21
Graphene Coatings for Biomedical Implants
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Cited by 37 •
2013
Graphene offers potential as a coating material for biomedical implants. In this study we demonstrate a method for coating nitinol alloys with nanometer thick layers of graphene and determine how graphene may influence implant response.
01:33
Coat Assembly and GTPases
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2023
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...
FAQs
Adaptor proteins provide the molecular connection between activated cargo receptors and clathrin. This linkage helps concentrate selected molecules at particular plasma-membrane regions rather than internalizing membrane contents indiscriminately. Because receptor activation precedes adaptor-mediated recruitment, the pathway can regulate which cargo enters the cell and connect uptake to receptor signaling in immune cells.
Clathrin triskelion units assemble into a lattice on the cytoplasmic side of the membrane, promoting curvature and formation of an invaginated vesicle. Dynamin acts at a later stage to help sever that vesicle from the cell surface. Separating membrane bending from vesicle release clarifies why both lattice assembly and dynamin activity are needed for efficient internalization.
Selectivity allows cells to internalize activated cargo receptors and their associated molecules in a controlled way. This is especially relevant to immune cells, where receptor trafficking can influence antigen-receptor availability and communication between cells. The pathway therefore does more than move membrane material: it helps connect extracellular recognition with changes in cellular organization and signaling.
A useful conceptual sequence begins with cargo-receptor activation, followed by adaptor recruitment and attachment to clathrin. Clathrin assembly then bends the membrane into an invagination, after which dynamin helps release the vesicle. Examining these stages separately helps identify whether a change affects cargo selection, lattice formation, membrane deformation, or vesicle scission.
In immune systems, this pathway contributes to antigen-receptor trafficking, nutrient uptake, and communication between immune cells. These roles link membrane internalization to receptor availability and cellular interactions. Studying the pathway can therefore help explain how immune cells regulate surface receptors and acquire material needed for their activities, while keeping the focus on trafficking rather than uptake alone.
Viruses, bacteria, and toxins can exploit clathrin-dependent routes to gain entry into cells. Their use of this cellular machinery makes clathrin-coated pits relevant to infection research as well as cell biology. Mapping the shared entry pathway can help investigators study pathogen invasion and identify points in the process that may represent potential therapeutic targets.