Sec6/8 Complex Is Recruited to Cell–Cell Contacts and Specifies Transport Vesicle Delivery to the Basal-Lateral Membrane in Epithelial Cells

• Published in: Cell Vol. 93; no. 5; pp. 731 - 740
• Main Authors: Grindstaff, Kent K, Yeaman, Charles, Anandasabapathy, Niroshana, Hsu, Shu-Chan, Rodriguez-Boulan, Enrique, Scheller, Richard H, Nelson, W.James
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 29.05.1998
• Subjects: Animals; Biological Transport; Carrier Proteins - metabolism; Cell Adhesion Molecules - metabolism; Cell Compartmentation; Cell Membrane - metabolism; Cell Polarity - physiology; Dogs; Epithelial Cells - metabolism; Golgi Apparatus - metabolism; Intercellular Junctions - physiology; Intracellular Membranes - metabolism; Kidney - cytology; Lipoproteins, LDL - metabolism; Molecular Weight; Nerve Growth Factors - metabolism; Protein Binding; Saccharomyces cerevisiae; Sec6/8 protein complex

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, ∼17S complex in nonpolarized MDCK epithelial cells. Upon initiation of calcium-dependent cell–cell adhesion, ∼70%...