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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.

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Affiliations

  • 1. Department of Molecular and Cellular Physiology, Stanford University School of Medicine, California 94305-5345, USA.
      Authors
    • Grindstaff KK 1
    (1 author)

ORCIDs linked to this article

Cell, 01 May 1998, 93(5):731-740
https://doi.org/10.1016/s0092-8674(00)81435-x PMID: 9630218 

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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Read article at publisher's site: https://doi.org/10.1016/s0092-8674(00)81435-x

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NIDDK NIH HHS (1)

NIGMS NIH HHS (3)