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

Overview

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.

publication date

  • May 29, 1998

Research

keywords

  • Carrier Proteins
  • Cell Adhesion Molecules
  • Cell Polarity
  • Epithelial Cells
  • Intercellular Junctions

Identity

Scopus Document Identifier

  • 0032577562

Digital Object Identifier (DOI)

  • 10.1016/s0092-8674(00)81435-x

PubMed ID

  • 9630218

Additional Document Info

volume

  • 93

issue

  • 5