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pubmed-article:9630218pubmed:abstractTextIn budding yeast, the Sec6/8p complex is essential for generating cell polarity by specifying vesicle delivery to the bud tip. We show that Sec6/8 homologs are components of a cytosolic, approximately 17S complex in nonpolarized MDCK epithelial cells. Upon initiation of calcium-dependent cell-cell adhesion, approximately 70% of Sec6/8 is rapidly (t(1/2) approximately 3-6 hr) recruited to sites of cell-cell contact. In streptolysin-O-permeabilized MDCK cells, Sec8 antibodies inhibit delivery of LDL receptor to the basal-lateral membrane, but not p75NTR to the apical membrane. These results indicate that lateral membrane recruitment of the Sec6/8 complex is a consequence of cell-cell adhesion and is essential for the biogenesis of epithelial cell surface polarity.lld:pubmed
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pubmed-article:9630218pubmed:dateRevised2011-3-18lld:pubmed
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pubmed-article:9630218pubmed:articleTitleSec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells.lld:pubmed
pubmed-article:9630218pubmed:affiliationDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, California 94305-5345, USA.lld:pubmed
pubmed-article:9630218pubmed:publicationTypeJournal Articlelld:pubmed
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