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Related Concept Videos

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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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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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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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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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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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Architecture of the caveolar coat complex.

Alexander Ludwig1, Benjamin James Nichols2, Sara Sandin3

  • 1School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551 Singapore aludwig@ntu.edu.sg.

Journal of Cell Science
|July 3, 2016
PubMed
Summary

The large caveolar coat complex (80S-CCC) forms a hollow sphere, dictating the shape of caveolae. This structure, composed of caveolins and cavins, ensures the stability of these essential membrane domains.

Keywords:
CaveolaeCaveolar coatCaveolinCavinCryo-electron tomography

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biophysics

Background:

  • Caveolae are vital membrane microdomains in endothelial, adipocyte, and muscle cells.
  • Caveolins and cavins are essential proteins for caveolae formation.
  • These proteins assemble into the large (80S) caveolar coat complex (80S-CCC).

Purpose of the Study:

  • To analyze the architecture of the 80S-CCC.
  • To understand how the 80S-CCC influences caveolae morphology.

Main Methods:

  • Isolation of 80S-CCC from mammalian cells.
  • Negative stain electron microscopy.
  • 3D cryo-electron tomography.

Main Results:

  • The 80S-CCC is a hollow sphere (50-80 nm diameter), matching caveolar bulb size.
  • The complex has a two-layered structure: an inner caveolin cage and an outer cavin coat.
  • The cavin coat aligns with the inner cage, suggesting a mechanism for coat stabilization.

Conclusions:

  • The 80S-CCC's spherical shape directly determines caveolae membrane morphology.
  • The dual-layered structure of caveolins and cavins provides a stable framework for caveolae.
  • This structural insight clarifies the formation and stability of caveolae.