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Related Concept Videos

Tight Junctions01:29

Tight Junctions

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Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
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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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Structural Protein Function01:56

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
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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 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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Mechanisms of Membrane Domain Formation00:59

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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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Updated: Dec 30, 2025

A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters
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Computational Modeling of Claudin Structure and Function.

Shadi Fuladi1, Ridaka-Wal Jannat1, Le Shen2,3

  • 1Department of Physics, University of Illinois at Chicago, Chicago, IL 60607, USA.

International Journal of Molecular Sciences
|January 26, 2020
PubMed
Summary
This summary is machine-generated.

This review explores computational models of claudins, focusing on how these proteins form selective ion channels within tight junctions to regulate epithelial and endothelial barrier function.

Keywords:
claudinion channelion transportmolecular dynamicstight junction

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Area of Science:

  • Biophysics
  • Cell Biology
  • Computational Biology

Background:

  • Tight junctions regulate paracellular transport across epithelia and endothelia.
  • Claudins are key structural and functional components of tight junctions, forming selective ion channels.
  • Recent crystallographic data offer insights into claudin structure and function.

Purpose of the Study:

  • To review computational and mathematical modeling approaches for understanding claudin barrier function.
  • To examine the role of claudin pores in epithelial barrier dynamics.
  • To present a functional model of claudin channels based on molecular dynamics.

Main Methods:

  • Review of computational and theoretical modeling studies.
  • Analysis of atomic-level descriptions of claudin pores.
  • Molecular dynamics simulations of claudin structure and function.

Main Results:

  • Computational models provide atomic-level insights into claudin channel selectivity.
  • Dynamic modeling elucidates the contribution of claudin pores to epithelial barrier function.
  • Molecular dynamics studies advance functional models of claudin channels.

Conclusions:

  • Computational and mathematical modeling are crucial for understanding claudin-mediated transport.
  • These models enhance our comprehension of epithelial barrier regulation by claudins.
  • Further integration of structural and dynamic data will refine claudin channel models.