Clathrin Adaptor Interaction
Clathrin Adaptor Interaction - Related Videos
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.
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...
12:40
Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
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Cited by 6 •
2014
Clathrin-mediated endocytosis, a rapid and highly dynamic process internalizes many proteins, including signaling receptors. The protocol described here directly visualizes the kinetics of individual endocytic events. This is essential for understanding how core members of the endocytic machinery coordinate with each other, and how protein cargo influence this process.
03:28
Labeling Murine T Helper Lymphocytes using Radiolabeled Monoclonal Antibodies
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2025
In this video, we demonstrate the intracellular radiolabeling of T helper cells using radioactive isotope-conjugated monoclonal antibodies for non-invasive positron emission tomography imaging.
06:41
Assessment of Social Interaction Behaviors
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Cited by 561 •
2011
Here we describe a detailed protocol for examination of sociability in mice by using Crawley's sociability and preference for social novelty test. We describe the advantages and possible applications for this procedure, including critical details important for correct interpretation of the results.
FAQs
Adaptor proteins act as a molecular link between three events: identifying cargo, associating with the membrane, and recruiting clathrin. This coordination concentrates selected molecules at a defined membrane site before the coated pit buds. Consequently, internalization is not simply bulk membrane uptake; it is organized around adaptor-controlled selection and coat assembly.
Two signals contribute to recruitment: sorting motifs on cargo molecules and membrane phosphoinositides recognized by adaptor complexes such as AP complexes. Cargo motifs provide information about which proteins should be transported, while phosphoinositides help position the adaptors at the appropriate membrane. Their combined recognition supports selective receptor internalization and trafficking.
Cargo selection identifies the molecules that should enter a transport carrier, whereas clathrin recruitment helps assemble the coated structure that supports vesicle formation. Adaptor proteins connect these functions without making them identical. This distinction helps explain how a cell can regulate both the contents of a vesicle and the membrane remodeling associated with its production.
An analysis can follow the sequence from adaptor association with membrane phosphoinositides, to recognition of cargo sorting motifs, to clathrin recruitment and coated-pit assembly. The final event to evaluate is budding from the plasma membrane. Tracking this order helps relate molecular binding events to receptor internalization and movement between membrane compartments.
This subject provides a framework for examining receptor internalization, nutrient uptake, signaling, and the distribution of proteins within cells. Because adaptor complexes help determine which materials enter transport carriers, changes in their interactions can alter both the movement of specific receptors and the organization of intracellular trafficking. These outcomes connect molecular mechanisms with broader cell behavior.
Researchers can use the interaction framework to ask whether a defect affects cargo recognition, membrane association, clathrin recruitment, coated-pit formation, or vesicle budding. Comparing these stages helps connect an altered molecular interaction with impaired receptor internalization or protein distribution. Such analysis is relevant to disease research because trafficking defects can disrupt signaling and transport between membrane compartments.