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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...

Endocytosis

Endocytosis

Eukaryotic cells acquire nutrients for growth and proliferation. Nutrients and other molecules that require degradation are internalized from the extracellular space by a process called endocytosis. The term ‘endocytosis' was first coined by Christian de Duve in 1963.
Endocytosis always begins with the plasma membrane enclosing an incoming molecule to form a transport vesicle which, in some cases, can be coated with a protein called ‘clathrin.' Endocytosed material is either sorted through...

Receptor-mediated Endocytosis

Receptor-mediated Endocytosis

Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...

Receptor-Mediated Endocytosis

Receptor-Mediated Endocytosis

Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...

Receptor-mediated Endocytosis

Receptor-mediated Endocytosis

Tail-anchoring of Proteins in the ER Membrane

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...

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Related Experiment Video

Updated: Jun 15, 2026

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

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

Published on: October 20, 2014

A screen for endocytic motifs.

Patrycja Kozik¹, Richard W Francis, Matthew N J Seaman

¹University of Cambridge, Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK.

Traffic (Copenhagen, Denmark)

|March 11, 2010

Summary

Researchers discovered new protein motifs involved in clathrin-mediated endocytosis, expanding the known signals beyond the three established types. This finding enhances our understanding of cellular cargo sorting mechanisms.

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Area of Science:

Cell Biology
Molecular Biology
Protein Trafficking

Background:

Cellular cargo selection into coated vesicles relies on short linear sorting motifs.
Three primary motifs for clathrin-mediated endocytosis are known: YXXPhi, [D/E]XXXL[L/I], and FXNPXY.

Purpose of the Study:

To identify novel endocytic motifs beyond the currently characterized ones.
To investigate the diversity of protein sequences involved in cellular internalization processes.

Main Methods:

Construction of a CD8 chimera library with random cytoplasmic tail sequences.
Utilized a fluorescence-activated cell sorting (FACS)-based assay for selection of endocytosed constructs.
Analysis of highly internalized sequences for motif identification.

Main Results:

Five highly internalized cytoplasmic tails were identified; only one contained a conventional motif.
Two tails revealed dileucine-like sequences, suggesting variations of the [D/E]XXXL[L/I] motif.
A novel internalization signal, YXXXPhiN, was discovered, functioning independently of the YXXPhi pathway.

Conclusions:

The repertoire of endocytic motifs is more extensive than previously known.
The YXXXPhiN motif represents a new class of sorting signal for clathrin-mediated endocytosis.
Similar novel motifs are found in endogenous proteins like CTLA-4, highlighting their biological relevance.