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First published online 6 January 2004
doi: 10.1242/jcs.00893

Journal of Cell Science 117, 559-570 (2004)
Published by The Company of Biologists 2004
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Research Article

Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells

Charles Yeaman*,{ddagger}, Kent K. Grindstaff and W. James Nelson

Department of Molecular and Cellular Physiology, Beckman Center for Molecular and Genetic Medicine, Stanford University School of Medicine, Stanford, CA 94305-5345, USA

{ddagger} Author for correspondence (e-mail: charles-yeaman{at}uiowa.edu)

Accepted 18 September 2003

Sec6/8 (exocyst) complex regulates vesicle delivery and polarized membrane growth in a variety of cells, but mechanisms regulating Sec6/8 localization are unknown. In epithelial cells, Sec6/8 complex is recruited to cell-cell contacts with a mixture of junctional proteins, but then sorts out to the apex of the lateral membrane with components of tight junction and nectin complexes. Sec6/8 complex fractionates in a high molecular mass complex with tight junction proteins and a portion of E-cadherin, and co-immunoprecipitates with cell surface-labeled E-cadherin and nectin-2{alpha}. Recruitment of Sec6/8 complex to cell-cell contacts can be achieved in fibroblasts when E-cadherin and nectin-2{alpha} are co-expressed. These results support a model in which localized recruitment of Sec6/8 complex to the plasma membrane by specific cell-cell adhesion complexes defines a site for vesicle delivery and polarized membrane growth during development of epithelial cell polarity.

Key words: Cell polarity, Cell membrane, Intercellular junctions, Intracellular membranes, Metabolism


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