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Related Concept Videos

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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Clathrin Coated Vesicles01:12

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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

Vesicular Tubular Clusters

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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.
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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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Transport Across the Golgi01:26

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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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Rab Cascades01:25

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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Related Experiment Video

Updated: Nov 10, 2025

In vivo and in vitro Studies of Adaptor-clathrin Interaction
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Atg27p co-fractionates with clathrin-coated vesicles in budding yeast.

Verónica A Segarra1, Anupam Sharma2, Sandra K Lemmon3

  • 1Department of Biology, High Point University, High Point, NC, USA 27268.

Micropublication Biology
|April 5, 2021
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Summary

Atg27p protein is trafficked within clathrin-coated vesicles (CCVs), confirmed by mass spectrometry and immunoblotting. This finding clarifies the transport mechanism for Atg27p in cellular pathways.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Autophagy Research

Background:

  • Atg27p is a transmembrane protein involved in autophagy.
  • It localizes to various cellular compartments, including endosomes and the Golgi.
  • Its C-terminus has motifs suggesting involvement in vesicular transport.

Purpose of the Study:

  • To investigate the role of clathrin-coated vesicles (CCVs) in Atg27p trafficking.
  • To confirm Atg27p as a component of CCVs.

Main Methods:

  • Mass spectrometry analysis of CCVs.
  • Immunoblotting to detect Atg27p in CCVs.
  • Analysis of CCVs from wild-type and auxilin-depleted cells.

Main Results:

  • Atg27p was identified in CCVs via mass spectrometry in previous studies.
  • Current study confirms Atg27p presence in CCVs using immunoblotting and further mass spectrometry.
  • This validates Atg27p as a cargo of CCVs.

Conclusions:

  • Atg27p is definitively a component of clathrin-coated vesicles.
  • This supports the role of CCVs in the transport of Atg27p within the endomembrane system.
  • Understanding Atg27p trafficking enhances knowledge of autophagy and endosomal sorting mechanisms.