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Related Concept Videos

Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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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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Vesicular Tubular Clusters01:45

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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...
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Transport Across the Golgi01:26

Transport Across the Golgi

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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...
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Coat Assembly and GTPases01:33

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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.
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Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

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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.
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Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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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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Related Experiment Video

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Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
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Clathrin and post-Golgi trafficking: a very complicated issue.

David G Robinson1, Peter Pimpl2

  • 1Centre for Organismal Studies (COS), University of Heidelberg, Heidelberg, Germany.

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|November 23, 2013
PubMed
Summary

Clathrin-coated vesicles (CCVs) assemble at the trans-Golgi network (TGN), but their function remains unclear. Studies on AP1M mutations do not confirm CCVs mediate vacuolar protein export from the TGN.

Keywords:
TGN maturationadaptor mutantsclathrin-coated vesiclesvacuolar protein transport

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In vivo and in vitro Studies of Adaptor-clathrin Interaction
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In vivo and in vitro Studies of Adaptor-clathrin Interaction

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • Clathrin-coated vesicles (CCVs) are crucial for endocytosis at the plasma membrane.
  • CCVs also assemble at the trans-Golgi network (TGN), but their specific role there is not well understood.
  • Adaptor protein 1 (AP1) complexes, including the μ-adaptin subunit AP1M, are involved in TGN vesicle formation.

Purpose of the Study:

  • To investigate the function of CCVs at the trans-Golgi network (TGN).
  • To clarify the role of AP1M in vacuolar and secretory protein transport.
  • To determine if CCVs mediate receptor-mediated export of vacuolar proteins from the TGN.

Main Methods:

  • Analysis of knockout mutations in the AP1M subunit of adaptor protein 1.
  • Examination of vacuolar and secretory protein transport pathways.
  • Evaluation of potential roles for TGN maturation in protein transport.

Main Results:

  • AP1M mutations disrupt multiple TGN trafficking pathways.
  • These mutations do not provide conclusive evidence for CCVs mediating vacuolar protein export.
  • Alternative mechanisms, such as TGN maturation, could account for vacuolar protein transport.

Conclusions:

  • The precise function of CCVs at the TGN is still uncertain.
  • AP1M knockout studies are insufficient to establish CCVs as mediators of vacuolar protein export.
  • Vacuolar protein transport may occur via TGN maturation and subsequent fusion with the vacuole.