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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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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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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

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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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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Selective membrane wrapping on differently sized nanoparticles regulated by clathrin assembly: A computational model.

Ye Li1, Man Zhang1, Xinhui Niu1

  • 1National Engineering Laboratory for Tree Breeding, College of Biological Sciences and Technology, Beijing Forestry University, Beijing 100083, China; Key Laboratory of Genetics and Breeding in Forest Trees and Ornamental Plants, Ministry of Education, College of Biological Sciences and Technology, Beijing Forestry University, Beijing 100083, China.

Colloids and Surfaces. B, Biointerfaces
|April 2, 2022
PubMed
Summary

Computer simulations reveal how clathrin influences nanoparticle (NP) uptake by cells. Clathrin modulates NP size selectivity during endocytosis, impacting cellular interactions and guiding future NP designs for biomedical uses.

Keywords:
Clathrin assemblyComputer simulationEndocytosisNanoparticleSize selectivity

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Area of Science:

  • Cellular Biology
  • Nanotechnology
  • Biophysics

Background:

  • Nanoparticle (NP) uptake into cells occurs through various pathways, with size being a critical determinant.
  • Clathrin-mediated endocytosis shows size selectivity for NPs, but the underlying molecular mechanisms are not fully understood, especially in vivo.

Purpose of the Study:

  • To investigate the role of clathrin in modulating nanoparticle size selectivity during cellular uptake.
  • To elucidate the molecular mechanisms governing NP-cell membrane interactions influenced by clathrin.

Main Methods:

  • Utilized computer simulations to model membrane wrapping around nanoparticles of varying sizes.
  • Mimicked clathrin assembly on the membrane to analyze its effect on NP wrapping dynamics.

Main Results:

  • Pure membranes readily wrap larger NPs, while clathrin actively modulates this process, tuning size selectivity.
  • Clathrin assembly facilitates wrapping for smaller NPs via curvature but hinders larger NPs due to size mismatch and membrane rigidification.
  • The interplay between NP size, NP-membrane adhesion, clathrin concentration, and NP distance dictates wrapping outcomes.

Conclusions:

  • Clathrin significantly alters nanoparticle-cell membrane interactions, influencing uptake pathways.
  • Understanding these complex interactions is crucial for designing nanoparticles with controlled cellular uptake for biomedical applications.