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Related Concept Videos

Receptor-mediated Endocytosis01:20

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 Endocytosis01:38

Receptor-mediated Endocytosis

Overview
Receptor-Mediated Endocytosis01:20

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...
Endocytosis01:16

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...
The Early Endosome: Endocytosis of Transferrin01:28

The Early Endosome: Endocytosis of Transferrin

Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
ER Retrieval Pathway01:45

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...

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Related Experiment Video

Updated: Jul 7, 2026

Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast
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Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast

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Endocytosis: biochemical analyses.

T E McGraw1, A Subtil

  • 1Weill Medical School of Cornell University, New York, New York, USA.

Current Protocols in Cell Biology
|January 30, 2008
PubMed
Summary
This summary is machine-generated.

Researchers developed methods to track cell surface proteins using post-translational modifications. This helps identify proteins that reach the cell surface or enter endocytic pathways for cellular communication.

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Last Updated: Jul 7, 2026

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • Integral membrane proteins synthesized in the endoplasmic reticulum are transported to the cell surface.
  • Post-translational modifications during Golgi transit serve as markers for cell surface proteins.
  • Understanding protein localization is crucial for cell-environment interactions.

Purpose of the Study:

  • To describe methods for identifying and tracking cell surface proteins.
  • To differentiate between proteins resident at the cell surface and those entering the endocytic pathway.

Main Methods:

  • Utilizing post-translational modifications (e.g., sialic acids) to track proteins.
  • Employing enzymatic treatments (sialidase, protease) and biotinylation to label cell surface proteins.
  • Differentiating endocytic versus surface-resident proteins by temperature-dependent treatments (4°C vs. 37°C).

Main Results:

  • Sialic acid analysis at 4°C identifies cell surface-resident proteins.
  • Temperature-dependent internalization of sialidase distinguishes endocytic pathway proteins.
  • Enzymatic and chemical labeling methods effectively identify cell surface-localized proteins.

Conclusions:

  • Post-translational modifications provide reliable markers for cell surface protein localization.
  • Temperature-controlled enzymatic assays can differentiate protein trafficking routes.
  • These methods enhance the study of cell surface protein dynamics and function.