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Vol. 15, Issue 6, 2639-2651, June 2004
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Epithelial Pathobiology Research Unit, Department of Pathology and Laboratory Medicine, Emory University, Atlanta, Georgia 30322
Submitted February 29, 2004;
Accepted March 15, 2004
Monitoring Editor: Daniel Goodenough
Disassembly of the epithelial apical junctional complex (AJC), composed of the tight junction (TJ) and adherens junction (AJ), is important for normal tissue remodeling and pathogen-induced disruption of epithelial barriers. Using a calcium depletion model in T84 epithelial cells, we previously found that disassembly of the AJC results in endocytosis of AJ/TJ proteins. In the present study, we investigated the role of the actin cytoskeleton in disassembly and internalization of the AJC. Calcium depletion induced reorganization of apical F-actin into contractile rings. Internalized AJ/TJ proteins colocalized with these rings. Both depolymerization and stabilization of F-actin inhibited ring formation and disassembly of the AJC, suggesting a role for actin filament turnover. Actin reorganization was accompanied by activation (dephosphorylation) of cofilin-1 and its translocation to the F-actin rings. In addition, Arp3 and cortactin colocalized with these rings. F-actin reorganization and disassembly of the AJC were blocked by blebbistatin, an inhibitor of nonmuscle myosin II. Myosin IIA was expressed in T84 cells and colocalized with F-actin rings. We conclude that disassembly of the AJC in calcium-depleted cells is driven by reorganization of apical F-actin. Mechanisms of such reorganization involve cofilin-1-dependent depolymerization and Arp2/3-assisted repolymerization of actin filaments as well as myosin IIA-mediated contraction.
Abbreviations used: ADF, actin-depolymerizing factor; AJ, adherens junction; Arp2/3, actin related proteins 2/3; BDM, 2,3-butanedione monoxime; JAM, junctional adhesion molecule, MNMM, mammalian nonmuscle myosin, PFA, paraformaldehyde; RMLC, regulatory myosin light chain; TEER, transepithelial electrical resistance; TJ, tight junction; TX-100, Triton X-100.
* Corresponding author. E-mail address: aiivano{at}emory.edu.
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