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Related Experiment Videos

Cytoskeletal interactions regulate inducible L-selectin clustering.

Polly E Mattila1, Chad E Green, Ulrich Schaff

  • 1Department of Veterinary and Biomedical Sciences, University of Minnesota, St. Paul, MN 55108, USA.

American Journal of Physiology. Cell Physiology
|March 25, 2005
PubMed
Summary

L-selectin (CD62L) mobility, crucial for neutrophil function in inflammation, is regulated by the actin cytoskeleton. This interaction enhances L-selectin

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Area of Science:

  • Immunology
  • Cell Biology
  • Biophysics

Background:

  • L-selectin (CD62L) is vital for neutrophil recruitment to inflammatory sites.
  • L-selectin clustering increases adhesiveness and signaling, but its mobility regulation is unclear.
  • Neutrophil stimulation alters plasma membrane organization into specific domains.

Purpose of the Study:

  • To investigate the molecular mechanisms regulating L-selectin lateral mobility.
  • To understand the role of the actin cytoskeleton and membrane domains in L-selectin function.

Main Methods:

  • Studied L-selectin clustering and colocalization with membrane proteins (CD55, CD45, CD11c).
  • Investigated the effect of microfilament disruption and cytoplasmic motif removal on L-selectin mobility.

Related Experiment Videos

  • Assessed L-selectin-dependent tethering under shear flow.

    • Main Results:

    • L-selectin clustered with GPI-anchored CD55, excluding CD45 and CD11c.
    • Disrupting microfilaments or altering the cationic motif increased L-selectin mobility and domain localization.
    • The cationic motif was essential for L-selectin-mediated tethering.

    Conclusions:

    • L-selectin lateral mobility is regulated by interactions with the actin cytoskeleton.
    • Actin cytoskeleton interactions enhance L-selectin-mediated leukocyte tethering.
    • Dynamic associations with membrane domains and cytoskeleton regulate L-selectin's effector functions.