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MBC in Press, published online ahead of print June 29, 2005
Mol. Biol. Cell 10.1091/mbc.E05-03-0242

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Submitted on March 22, 2005
Accepted on June 20, 2005

Intermediate Filaments Interact with Dormant Ezrin in Intestinal Epithelial Cells

Flavia A. Wald,* Andrea S. Oriolo,* M. Llanos Casanova,{dagger} and Pedro J.I. Salas*

*Department of Cell Biology and Anatomy R-124, University of Miami School of Medicine, Miami, FL 33101; {dagger}CIEMAT, University Complutense, E-28040 Madrid, Spain

Monitoring Editor: M. Bishr Omary

Ezrin connects the apical F-actin scaffold to membrane proteins in the apical brush border of intestinal epithelial cells. Yet, the mechanisms that recruit ezrin to the apical domain remain obscure. Using stable CACO-2 transfectants expressing keratin 8 (K8) antisense RNA under a tetracycline responsive element, we showed that the actin-ezrin scaffold cannot assemble in the absence of intermediate filaments (IFs). Overexpression of ezrin partially rescued this phenotype. Overexpression of K8 in mice also disrupted the assembly of the brush border, but ezrin distributed away from the apical membrane in spots along supernumerary IFs. In cytochalasin D-treated cells ezrin localized to a subapical compartment and coimmunoprecipitated with IFs. Overexpression of ezrin in undifferentiated cells showed a Triton-insoluble ezrin compartment negative for phospho-T567 (dormant) ezrin visualized as spots along IFs. Pulse-chase analysis showed that Triton-insoluble newly synthesized ezrin transiently coimmunoprecipitates with IFs during the first 30 min of the chase. Dormant, but not active (p-T567), ezrin bound in vitro to isolated denatured keratins in Far-Western analysis, and to native IFs in pull down assays. We conclude that a transient association to IFs is an early step in the polarized assembly of apical ezrin in intestinal epithelial cells.

Address correspondence to: Pedro J.I. Salas (psalas{at}miami.edu)




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