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Updated: May 5, 2026

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
Published on: October 20, 2014
Clathrin and post-Golgi trafficking: a very complicated issue
David G Robinson1, Peter Pimpl2
1Centre for Organismal Studies (COS), University of Heidelberg, Heidelberg, Germany.
Abstract:
Clathrin-coated vesicles (CCVs) are formed at the plasma membrane and act as vectors for endocytosis. They also assemble at the trans-Golgi network (TGN), but their exact function at this organelle is unclear. Recent studies have examined the effects on vacuolar and secretory protein transport of knockout mutations of the adaptor protein 1 (AP1) μ-adaptin subunit AP1M, but these investigations do not clarify the situation. These mutations lead to the abrogation of multiple trafficking pathways at the TGN and cannot be used as evidence in favour of CCVs being agents for receptor-mediated export of vacuolar proteins out of the TGN. This transport process could just as easily occur through the maturation of the TGN into intermediate compartments that subsequently fuse with the vacuole.
Insights
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.
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.
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