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Am J Physiol Cell Physiol 283: C489-C499, 2002. First published March 20, 2002; doi:10.1152/ajpcell.00566.2001
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Vol. 283, Issue 2, C489-C499, August 2002

Protein kinase C regulates endocytosis and recycling of E-cadherin

Tam Luan Le1,2, Shannon R. Joseph1, Alpha S. Yap1,3, and Jennifer L. Stow1,2

1 Institute for Molecular Bioscience, 2 Department of Biochemistry, and 3 Department of Physiology and Pharmacology, University of Queensland, Brisbane 4072, Queensland, Australia

E-cadherin is a major component of adherens junctions in epithelial cells. We showed previously that a pool of cell surface E-cadherin is constitutively internalized and recycled back to the surface. In the present study, we investigated the potential role of protein kinase C (PKC) in regulating the trafficking of surface E-cadherin in Madin-Darby canine kidney cells. Using surface biotinylation and immunofluorescence, we found that treatment of cells with phorbol esters increased the rate of endocytosis of E-cadherin, resulting in accumulation of E-cadherin in apically localized early or recycling endosomes. The recycling of E-cadherin back to the surface was also decreased in the presence of phorbol esters. Phorbol ester-induced endocytosis of E-cadherin was blocked by specific inhibitors, implicating novel PKC isozymes, such as PKC-epsilon in this pathway. PKC activation led to changes in the actin cytoskeleton facilitating E-cadherin endocytosis. Depolymerization of actin increased endocytosis of E-cadherin, whereas the PKC-induced uptake of E-cadherin was blocked by the actin stabilizer jasplakinolide. Our findings show that PKC regulates vital steps of E-cadherin trafficking, its endocytosis, and its recycling.

trafficking; cell-cell adhesion; actin


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