ARF6 Controls Post-Endocytic Recycling through Its Downstream Exocyst Complex Effector

• Published in: The Journal of cell biology Vol. 163; no. 5; pp. 1111 - 1121
• Main Authors: Prigent, Magali, Dubois, Thierry, Raposo, Graça, Derrien, Valérie, Tenza, Danièle, Rossé, Carine, Camonis, Jacques, Chavrier, Philippe
• Format: Journal Article
• Language: English
• Published: United States Rockefeller University Press 08.12.2003; The Rockefeller University Press
• Subjects: ADP-Ribosylation Factors - genetics; ADP-Ribosylation Factors - metabolism; Animals; Antibodies; B lymphocytes; Cell Line; Cell Membrane - metabolism; Cell membranes; Cell Nucleus - metabolism; Cells; Cellular biology; Cellular immunity; Cytoplasmic Vesicles - metabolism; Endocytosis - physiology; Endosomes - metabolism; Endosomes - ultrastructure; Epithelial cells; Fungal Proteins - genetics; Fungal Proteins - metabolism; Guanosine Triphosphate - metabolism; HeLa cells; Humans; Membranes; P branes; Plasma; Plasma interactions; Protein Transport; Recombinant Fusion Proteins - metabolism; Recycling; RNA, Small Interfering - metabolism; Saccharomyces cerevisiae Proteins; trans-Golgi Network - metabolism; trans-Golgi Network - ultrastructure; Transferrin - metabolism; Two-Hybrid System Techniques; Vesicular Transport Proteins
• ISSN: 0021-9525; 1540-8140
• DOI: 10.1083/jcb.200305029

The small guanosine triphosphate (GTP)-binding protein ADP-ribosylation factor (ARF) 6 regulates membrane recycling to regions of plasma membrane remodeling via the endocytic pathway. Here, we show that GTP-bound ARF6 interacts with Sec10, a subunit of the exocyst complex involved in docking of vesicles with the plasma membrane. We found that Sec10 localization in the perinuclear region is not restricted to the trans-Golgi network, but extends to recycling endosomes. In addition, we report that depletion of Sec5 exocyst subunit or dominant inhibition of Sec10 affects the function and the morphology of the recycling pathway. Sec10 is found to redistribute to ruffling areas of the plasma membrane in cells expressing GTP-ARF6, whereas dominant inhibition of Sec10 interferes with ARF6-induced cell spreading. Our paper suggests that ARF6 specifies delivery and insertion of recycling membranes to regions of dynamic reorganization of the plasma membrane through interaction with the vesicle-tethering exocyst complex.