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Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells

Grindstaff, Kent K, Yeaman, Charles, Anandasabapathy, Niroshana, Hsu, Shu-Chan, Rodriguez-Boulan, Enrique, Scheller, Richard H, Nelson, W.James·1998·Cell
DOI 10.1016/s0092-8674(00)81435-x
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Abstract

In 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.

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Metadata

Authors
Grindstaff, K. K., Yeaman, C., Anandasabapathy, N., Hsu, S.-C., Rodriguez-Boulan, E., Scheller, R. H., & Nelson, W. J.
Venue
Cell
Publisher
Elsevier BV
Published
1998-05
Volume
93
Issue
5
Pages
731-740
ISSN
0092-8674
DOI
10.1016/s0092-8674(00)81435-x
Cited by
460
References
0
Language
en
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