TY - JOUR T1 - A novel GTP-binding protein-adaptor protein complex responsible for export of Vangl2 from the trans Golgi network. JF - Elife Y1 - 2013 A1 - Yusong Guo A1 - Zanetti, Giulia A1 - Schekman, Randy KW - Adaptor Protein Complex 1 KW - Adaptor Protein Complex gamma Subunits KW - Adaptor Protein Complex mu Subunits KW - ADP-Ribosylation Factors KW - Amino Acid Sequence KW - Animals KW - Binding Sites KW - Cadherins KW - Cell Adhesion Molecules KW - Cell Polarity KW - Cercopithecus aethiops KW - COS Cells KW - Epithelial Cells KW - Frizzled Receptors KW - HeLa Cells KW - Humans KW - Intracellular Signaling Peptides and Proteins KW - Membrane Proteins KW - Molecular Sequence Data KW - Mutation KW - Phosphorylation KW - Protein Binding KW - Protein Interaction Domains and Motifs KW - Protein Kinase C KW - Protein Transport KW - Receptor Protein-Tyrosine Kinases KW - RNA Interference KW - trans-Golgi Network KW - Transfection AB -

Planar cell polarity (PCP) requires the asymmetric sorting of distinct signaling receptors to distal and proximal surfaces of polarized epithelial cells. We have examined the transport of one PCP signaling protein, Vangl2, from the trans Golgi network (TGN) in mammalian cells. Using siRNA knockdown experiments, we find that the GTP-binding protein, Arfrp1, and the clathrin adaptor complex 1 (AP-1) are required for Vangl2 transport from the TGN. In contrast, TGN export of Frizzled 6, which localizes to the opposing epithelial surface from Vangl2, does not depend on Arfrp1 or AP-1. Mutagenesis studies identified a YYXXF sorting signal in the C-terminal cytosolic domain of Vangl2 that is required for Vangl2 traffic and interaction with the μ subunit of AP-1. We propose that Arfrp1 exposes a binding site on AP-1 that recognizes the Vangl2 sorting motif for capture into a transport vesicle destined for the proximal surface of a polarized epithelial cell.DOI:http://dx.doi.org/10.7554/eLife.00160.001.

VL - 2 ER -