Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes
Copyright policy )Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes
Specific recognition of phosphoinositides is crucial for protein sorting and membrane trafficking. Protein transport to the yeast vacuole depends on the Vam7 t-SNARE and its phox homology (PX) domain. Here, we show that the PX domain of Vam7 targets to vacuoles in vivo in a manner dependent on phosphatidylinositol 3-phosphate generation. A novel phosphatidylinositol-3-phosphate-binding motif and an exposed loop that interacts with the lipid bilayer are identified by nuclear magnetic resonance spectroscopy. Conservation of key structural and binding site residues across the diverse PX family indicates a shared fold and phosphoinositide recognition function.
- University of California, San Diego United States
- University of California, San Diego United States
- University of Colorado Anschutz Medical Campus United States
- University of Colorado Cancer Center United States
Binding Sites, Saccharomyces cerevisiae Proteins, Synaptosomal-Associated Protein 25, Molecular Sequence Data, Membrane Proteins, Membranes, Artificial, Nerve Tissue Proteins, Intracellular Membranes, Saccharomyces cerevisiae, Protein Structure, Tertiary, Fungal Proteins, Protein Transport, Microscopy, Fluorescence, Phosphatidylinositol Phosphates, Amino Acid Sequence, Qc-SNARE Proteins, SNARE Proteins, Nuclear Magnetic Resonance, Biomolecular, Sequence Alignment, Protein Binding
Binding Sites, Saccharomyces cerevisiae Proteins, Synaptosomal-Associated Protein 25, Molecular Sequence Data, Membrane Proteins, Membranes, Artificial, Nerve Tissue Proteins, Intracellular Membranes, Saccharomyces cerevisiae, Protein Structure, Tertiary, Fungal Proteins, Protein Transport, Microscopy, Fluorescence, Phosphatidylinositol Phosphates, Amino Acid Sequence, Qc-SNARE Proteins, SNARE Proteins, Nuclear Magnetic Resonance, Biomolecular, Sequence Alignment, Protein Binding
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