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Related Concept Videos

Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation.  In gated transport, folded...
COP Coated Vesicles00:59

COP Coated Vesicles

Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of different...
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...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
Transport Across the Golgi01:26

Transport Across the Golgi

While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
Clathrin Coated Vesicles01:12

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...

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Related Experiment Video

Updated: Jul 5, 2026

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
12:40

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

Published on: October 20, 2014

Vps10p transport from the trans-Golgi network to the endosome is mediated by clathrin-coated vesicles.

O Deloche1, B G Yeung, G S Payne

  • 1Howard Hughes Medical Institute and Department of Molecular and Cell Biology, University of California, 229 Stanley Hall, Berkeley, California 94720-3206, USA.

Molecular Biology of the Cell
|February 17, 2001
PubMed
Summary

Clathrin-coated vesicles (CCVs) mediate vacuolar protein transport in yeast. Vps10p receptor sorting to the endosome is independent of direct clathrin interaction, suggesting CCVs facilitate transport.

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Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
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Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells

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Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells
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Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells

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Related Experiment Videos

Last Updated: Jul 5, 2026

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
12:40

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

Published on: October 20, 2014

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
11:05

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells

Published on: February 21, 2019

Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells
08:02

Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells

Published on: October 17, 2025

Area of Science:

  • Cell biology
  • Molecular biology
  • Yeast genetics

Background:

  • Vacuolar protein transport is crucial for cellular function.
  • Clathrin-coated vesicles (CCVs) are involved in protein sorting and trafficking.
  • The trans-Golgi network (TGN) and endosomes are key organelles in the secretory pathway.

Purpose of the Study:

  • To investigate the role of CCVs in vacuolar protein transport from the TGN to the endosome in Saccharomyces cerevisiae.
  • To determine the involvement of specific proteins, Apl2p and Vps10p, in CCV-mediated transport.
  • To elucidate the function of the Vps10p C-terminal domain in protein sorting.

Main Methods:

  • Native immunoisolation procedure.
  • Co-immunoprecipitation assays.
  • Analysis of yeast mutants (pep12 Delta, vps34 Delta, Vps10C(t) Delta p).

Main Results:

  • Apl2p and Vps10p associate with clathrin molecules.
  • Vps10p packaging into CCVs is reduced in pep12 Delta and vps34 Delta mutants.
  • Vps10p sorting is independent of Apl2p.
  • A Vps10p mutant lacking its C-terminal domain co-immunoprecipitates with clathrin.

Conclusions:

  • CCVs mediate Vps10p transport from the TGN to the endosome.
  • This transport is independent of direct Vps10p-clathrin interactions.
  • The Vps10p C-terminal domain is critical for retrieval from the prevacuolar compartment, not TGN sorting.