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Related Concept Videos

COP Coated Vesicles00:59

COP Coated Vesicles

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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...
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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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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.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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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.
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...
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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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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...
4.0K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

2.4K
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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Related Experiment Video

Updated: May 23, 2025

Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis
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Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis

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Organizing principles underlying COPII-mediated transport.

Julia R Flood1, Caitlin A Mendina1, Anjon Audhya1

  • 1Department of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI, 53706, USA.

Current Opinion in Cell Biology
|March 11, 2025
PubMed
Summary
This summary is machine-generated.

Coat Protein complex II (COPII) drives transport from the ER to ERGIC. Recent findings reveal how ER structure facilitates cargo export, independent of cytoskeletal guidance.

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Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
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Related Experiment Videos

Last Updated: May 23, 2025

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Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The early secretory pathway is crucial for protein and lipid transport from the endoplasmic reticulum (ER) to ER-Golgi Intermediate Compartments (ERGIC).
  • Coat Protein complex II (COPII) mediated transport is central to this process, involving the formation of transport intermediates at transitional ER (tER) sites.
  • Mechanisms regulating COPII-dependent trafficking and ER export dynamics remain incompletely understood.

Purpose of the Study:

  • To elucidate the structural organization of the ER that facilitates cargo export.
  • To understand how COPII-mediated transport operates within the early secretory pathway.
  • To highlight recent advancements in comprehending ER export mechanisms.

Main Methods:

  • Review of recent literature on COPII vesicle formation and function.
  • Analysis of ER subdomains and their role in cargo sorting.
  • Investigation of the physical constraints and transport dynamics within the ER-ERGIC lumen.

Main Results:

  • COPII machinery accumulates on specific ER subdomains (tER) to initiate transport.
  • Transport intermediates are generated with diverse sizes and shapes.
  • Cargo export occurs across a lumenal chasm without direct cytoskeletal involvement.

Conclusions:

  • The ER possesses inherent structural features that promote efficient cargo export.
  • COPII dynamics and ER architecture are coordinated to manage secretory flux.
  • Understanding these mechanisms provides insight into cellular protein trafficking regulation.