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MBC in Press, published online ahead of print December 27, 2007
Mol. Biol. Cell 10.1091/mbc.E07-06-0596

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Submitted on June 22, 2007
Revised on December 10, 2007
Accepted on December 19, 2007

Caveolin-1 and -2 Interact with Connexin43 and Regulate Gap Junctional Intercellular Communication in Keratinocytes

Stéphanie Langlois,* Kyle N. Cowan,*{dagger} Qing Shao,* Bryce J. Cowan,{ddagger} and Dale W. Laird*{sect}

Departments of *Anatomy and Cell Biology, {sect}Physiology and Pharmacology, and {dagger}Surgery, University of Western Ontario, London, ON, N6A 5C1, Canada; {ddagger}Department of Dermatology and Skin Science, University of British Columbia, Vancouver, BC, V5Z 4E8, Canada

Monitoring Editor: Robert Parton

Connexin43 (Cx43) has been reported to interact with caveolin-1 (Cav-1), but the role of this association and whether other members of the caveolin family bind Cx43 had yet to be established. In this study, we show that Cx43 coimmunoprecipitates and colocalizes with Cav-1 and Cav-2 in rat epidermal keratinocytes. The colocalization of Cx43 with Cav-1 was confirmed in keratinocytes from human epidermis in vivo. Our mutation and Far Western analyses revealed that the C-terminal tail of Cx43 is required for its association with Cavs and that the Cx43/Cav-1 interaction is direct. Our results indicate that newly synthesized Cx43 interacts with Cavs in the Golgi apparatus and that the Cx43/Cavs complex also exists at the plasma membrane in lipid rafts. Using overexpression and siRNA approaches, we demonstrated that caveolins regulate gap junctional intercellular communication (GJIC) and that the presence of Cx43 in lipid raft domains may contribute to the mechanism modulating GJIC. Our results suggest that the Cx43/Cavs association occurs during exocytic transport and clearly indicate that caveolin regulates GJIC.

Address correspondence to: Dale W. Laird (dale.laird{at}schulich.uwo.ca)




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[Abstract] [Full Text] [PDF]


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