A novel GTP-binding protein-adaptor protein complex responsible for export of Vangl2 from the trans Golgi network.
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.
Mesh Terms:
ADP-Ribosylation Factors, Adaptor Protein Complex 1, Adaptor Protein Complex gamma Subunits, Adaptor Protein Complex mu Subunits, Amino Acid Sequence, Animals, Binding Sites, COS Cells, Cadherins, Cell Adhesion Molecules, Cell Polarity, Cercopithecus aethiops, Epithelial Cells, Frizzled Receptors, HeLa Cells, Humans, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Molecular Sequence Data, Mutation, Phosphorylation, Protein Binding, Protein Interaction Domains and Motifs, Protein Kinase C, Protein Transport, RNA Interference, Receptor Protein-Tyrosine Kinases, Transfection, trans-Golgi Network
ADP-Ribosylation Factors, Adaptor Protein Complex 1, Adaptor Protein Complex gamma Subunits, Adaptor Protein Complex mu Subunits, Amino Acid Sequence, Animals, Binding Sites, COS Cells, Cadherins, Cell Adhesion Molecules, Cell Polarity, Cercopithecus aethiops, Epithelial Cells, Frizzled Receptors, HeLa Cells, Humans, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Molecular Sequence Data, Mutation, Phosphorylation, Protein Binding, Protein Interaction Domains and Motifs, Protein Kinase C, Protein Transport, RNA Interference, Receptor Protein-Tyrosine Kinases, Transfection, trans-Golgi Network
Elife
Date: Jan. 08, 2013
PubMed ID: 23326640
View in: Pubmed Google Scholar
Download Curated Data For This Publication
215845
Switch View:
- Interactions 5