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Related Experiment Videos

Actin depolymerization disrupts tight junctions via caveolae-mediated endocytosis.

Le Shen1, Jerrold R Turner

  • 1Department of Pathology, The University of Chicago, Chicago, IL 60637, USA.

Molecular Biology of the Cell
|June 17, 2005
PubMed
Summary
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Actin depolymerization disrupts epithelial barrier function by triggering tight junction (TJ) protein internalization. This process involves caveolae-mediated endocytosis, impacting TJ structure and barrier integrity.

Area of Science:

  • Cell biology
  • Epithelial biology
  • Membrane trafficking

Background:

  • Tight junctions (TJs) are crucial for epithelial barrier function.
  • Actin depolymerization is known to disrupt TJs, but the underlying mechanisms are unclear.

Purpose of the Study:

  • To elucidate the mechanisms by which actin depolymerization disrupts TJ structure and function.
  • To investigate the role of membrane trafficking in TJ disruption.

Main Methods:

  • Utilized Madin-Darby canine kidney (MDCK) cells expressing fluorescently tagged TJ proteins.
  • Employed time-lapse microscopy and transepithelial electrical resistance (TER) measurements.
  • Induced actin depolymerization with latrunculin A (LatA) and manipulated membrane traffic.

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Main Results:

  • LatA induced rapid loss of TER and occludin internalization.
  • Occludin internalization and TER loss were dependent on membrane traffic and occurred via caveolae-mediated endocytosis.
  • ZO-1 and claudin-1 redistribution occurred later, after maximal TER loss.

Conclusions:

  • Actin depolymerization disrupts TJ barrier function through caveolae-mediated endocytosis of TJ components like occludin.
  • Membrane trafficking plays a critical role in the disruption of TJ structure and function following actin depolymerization.