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Related Concept Videos

Pinching-off of Coated Vesicles01:32

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...
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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...
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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...
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Recycling Endosomes and Transcytosis00:58

Recycling Endosomes and Transcytosis

The recycling endosome, also known as the endosomal recycling compartment (ERC), is a part of the slow-recycling process of the endocytic pathway. Molecules internalized through receptor-mediated endocytosis are either degraded in the lysosomes or are recycled to the plasma membrane through the fast- or slow-recycling route.
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UNC119 inhibits dynamin and dynamin-dependent endocytic processes.

Zunayet Karim1, Ramarao Vepachedu, Magdalena Gorska

  • 1Division of Allergy and Immunology, Department of Medicine, National Jewish Health, 1400 Jackson Street, Denver, CO 80206, USA.

Cellular Signalling
|September 29, 2009
PubMed
Summary

Unc119 regulates cellular uptake by modulating endocytosis pathways. This adapter protein inhibits clathrin- and caveolae-mediated endocytosis and interacts with dynamin to control vesicular trafficking.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Unc119 is an adapter protein involved in tyrosine kinase activation in various cell types.
  • It plays a role in retinal photoreceptor synapses and has been shown to inhibit macropinocytosis.
  • Its precise role in diverse endocytic pathways remained unclear.

Purpose of the Study:

  • To investigate the role of Unc119 in clathrin- and caveolae-based endocytosis and macropinocytosis.
  • To elucidate the mechanism by which Unc119 regulates endocytic processes.
  • To determine the interaction of Unc119 with key endocytic machinery like dynamin.

Main Methods:

  • Depletion and overexpression of Unc119 in fibroblasts.
  • Assessing uptake of various cargo molecules (transferrin, FM4-64, albumin, viruses, ligand-coated beads, cholera toxin B).
  • Investigating protein-protein interactions and enzyme activity assays (Unc119-dynamin interaction, dynamin GTPase activity).

Main Results:

  • Unc119 depletion enhanced, while overexpression inhibited, clathrin- and caveolae-mediated endocytosis.
  • Unc119 showed an opposite effect on cholera toxin B uptake (a dynamin-independent pathway).
  • Unc119 binds to dynamin and inhibits its GTPase activity, reducing its interaction with amphiphysin.

Conclusions:

  • Unc119 acts as a regulator of multiple endocytic pathways, including clathrin- and caveolae-mediated endocytosis.
  • Unc119 modulates vesicular trafficking by interacting with and inhibiting dynamin's GTPase activity.
  • Unc119 establishes a threshold for endocytosis, influencing cellular uptake processes.