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Related Experiment Videos

Requirement of cortical actin organization for bombesin, endothelin, and EGF receptor internalization.

J A Lunn1, H Wong, E Rozengurt

  • 1Department of Medicine, School of Medicine, Center for Ulcer Research and Education Digestive Diseases Research Center and Molecular Biology Institute, University of California, Los Angeles, California 90095, USA.

American Journal of Physiology. Cell Physiology
|November 18, 2000
PubMed
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Latrunculin A inhibits actin polymerization, revealing that cortical actin is essential for receptor internalization. This process is independent of actin stress fibers disrupted by other agents.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The precise role of actin organization in receptor internalization upon ligand binding is not fully understood.
  • Receptor internalization is a critical process in cellular signaling and regulation.

Purpose of the Study:

  • To investigate the role of actin organization, specifically cortical actin, in occupancy-induced receptor internalization.
  • To determine whether actin stress fibers or cortical actin structures are essential for this process.

Main Methods:

  • Treatment of mouse Swiss 3T3 cells with latrunculin A, cytochalasin D, and Rho-kinase inhibitor HA-1077.
  • Assessing internalization of endogenous bombesin/gastrin-releasing peptide (GRP) receptor using radiolabeled GRP and fluorescently labeled bombesin.

Related Experiment Videos

  • Evaluating internalization of endothelin A receptor and epidermal growth factor receptor.
  • Main Results:

    • Latrunculin A significantly inhibited the internalization of the bombesin/GRP receptor, endothelin A receptor, and epidermal growth factor receptor.
    • Cytochalasin D and HA-1077 showed minimal or no inhibition of bombesin/GRP receptor internalization.
    • These findings suggest that latrunculin A-sensitive cortical actin, not stress fibers, is crucial for receptor internalization.

    Conclusions:

    • Cortical actin structures, sensitive to latrunculin A, are necessary for occupancy-induced receptor internalization in animal cells.
    • The study differentiates the roles of different actin structures in receptor trafficking.