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MBC in Press, published online ahead of print December 20, 2006
Mol. Biol. Cell 10.1091/mbc.E06-03-0201

A more recent version of this article appeared on March 1, 2007
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Submitted on March 14, 2006
Revised on November 3, 2006
Accepted on November 5, 2006

GCP6 Binds to Intermediate Filaments: A Novel Function of Keratins in the Organization of Microtubules in Epithelial Cells

Andrea S. Oriolo, Flavia A. Wald, Gisella Canessa, and Pedro J.I. Salas

Department of Cell Biology and Anatomy, University of Miami Miller School of Medicine, Miami, FL 33136

Monitoring Editor: M. Bishr Omary

In simple epithelial cells, attachment of MTOCs to IFs enables their localization to the apical domain. It is released by Cdk1 phosphorylation. Here, we identified a component of the {gamma}-tubulin ring complex, GCP6, as a keratin partner in yeast two-hybrid assays. This was validated by binding in vitro of both purified full-length HIS-tagged GCP6 and a GCP6(1397-1819) fragment to keratins, and pull-down with native IFs. Keratin binding was blocked by Cdk1-mediated phosphorylation of GCP6. GCP6 was apical in normal enterocytes but diffuse in K8-null cells. GCP6 knock-down with shRNAs in CACO-2 cells resulted in {gamma}-tubulin signal scattered throughout the cytoplasm, MTs in the perinuclear and basal regions, and microtubule-nucleating activity localized deep in the cytoplasm. Expression of a small fragment GCP6(1397-1513) that competes binding to keratins in vitro, displaced {gamma}-tubulin from the cytoskeleton, resulted in depolarization of {gamma}-tubulin, changes in the distribution of microtubules and microtubule-nucleation sites. Expression of a full-length S1397D mutant in the Cdk1 phosphorylation site delocalized centrosomes. We conclude that GCP6 participates in the attachment of MTOCs to IFs in epithelial cells and is among the factors that determine the peculiar architecture of microtubules in polarized epithelia.

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




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