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Clathrin Coated Vesicles

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 Vesicles

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...

Catenins

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...

Assembly of Signaling Complexes

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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.
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Coat Assembly and GTPases

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...

Regulation of Nuclear Protein Sorting

Regulation of Nuclear Protein Sorting

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Related Experiment Video

Updated: Jul 12, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

The NECAP PHear domain increases clathrin accessory protein binding potential.

Brigitte Ritter¹, Alexei Yu Denisov, Jacynthe Philie

¹Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada.

The EMBO Journal

|September 1, 2007

Summary

NECAP proteins bind accessory proteins using a novel PHear domain, distinct from the AP-2 alpha-ear. This discovery reveals a new mechanism for regulating clathrin-mediated endocytosis and protein recruitment.

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Published on: March 11, 2021

Area of Science:

Cell Biology
Molecular Biology
Structural Biology

Background:

Clathrin-mediated endocytosis (CME) is essential for cellular processes.
The AP-2 complex is a key regulator of CME, primarily through its alpha-ear domain.
Accessory proteins are recruited by AP-2 to facilitate CME.

Purpose of the Study:

To elucidate the structure and function of the N-terminal region of NECAP 1.
To investigate the interaction between NECAP 1 and accessory proteins.
To establish the role of NECAPs in clathrin-mediated endocytosis.

Main Methods:

X-ray crystallography to determine the structure of the NECAP 1 N-terminal region.
Site-directed mutagenesis to analyze FxDxF motif binding.
Functional assays, including knockdown of NECAP, to assess transferrin uptake.

Main Results:

The conserved N-terminal region of NECAP 1 forms a novel PHear domain.
The PHear domain binds accessory proteins with FxDxF motifs, previously thought to bind only to the AP-2 alpha-ear.
NECAP knockdown impairs transferrin uptake, confirming NECAPs' role in CME.

Conclusions:

NECAP 1 utilizes a unique PHear domain for FxDxF motif binding, distinct from the AP-2 alpha-ear.
This study reveals a convergence of distinct protein modules recognizing a common motif to regulate endocytosis.
NECAPs are functionally important for efficient clathrin-mediated endocytosis.