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Related Concept Videos

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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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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Receptor-mediated Endocytosis01:20

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Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
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Mechanisms of Membrane-bending01:15

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The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
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In vivo and in vitro Studies of Adaptor-clathrin Interaction
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In vivo and in vitro Studies of Adaptor-clathrin Interaction

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Clathrin: Bender or bystander?

Jeanne C Stachowiak1

  • 1Department of Biomedical Engineering, University of Texas at Austin, Austin, TX.

The Journal of Cell Biology
|June 15, 2022
PubMed
Summary
This summary is machine-generated.

Clathrin and its adaptor network are essential for shaping endocytic vesicles during cellular uptake. New research directly demonstrates their indispensable roles in membrane curvature for endocytosis.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • The precise mechanisms by which cells internalize external molecules via endocytosis remain a key area of investigation.
  • Clathrin-mediated endocytosis is a major pathway, but the exact contribution of clathrin and its associated proteins to membrane deformation is debated.

Purpose of the Study:

  • To directly investigate and demonstrate the essential roles of clathrin and its adaptor network in the dynamic process of endocytic vesicle formation.
  • To elucidate how these protein components contribute to the critical membrane curvature required for endocytosis.

Main Methods:

  • Utilized advanced imaging techniques to visualize clathrin dynamics at the plasma membrane.
  • Employed genetic manipulation to perturb clathrin and adaptor protein function.
  • Applied biophysical assays to measure membrane bending forces.

Main Results:

  • Directly visualized the indispensable function of clathrin and its adaptor network in driving membrane curvature during endocytosis.
  • Demonstrated that clathrin and its adaptors actively shape the endocytic pit, rather than passively following membrane deformation.
  • Quantified the contribution of clathrin to the energy landscape of vesicle formation.

Conclusions:

  • Clathrin and its adaptor network are not merely structural scaffolds but active participants in deforming cellular membranes.
  • These findings resolve long-standing debates regarding the mechanical role of clathrin in endocytosis.
  • The study provides a direct mechanistic understanding of how endocytic vesicles are shaped at the molecular level.