Article abstract
Nature Cell Biology 3, 613 - 618 (2001)
Published online: 24 May 2001 | doi:10.1038/35083000
Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes
Matthew L. Cheever1,4, Trey K. Sato4,3, Tonny de Beer2, Tatiana G. Kutateladze2, Scott D. Emr3 & Michael Overduin2
Abstract
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.
- Molecular Biology Program, University of Colorado Health Sciences Center, 4200 East Ninth Avenue, Denver, Colorado, 80262, USA
- Department of Pharmacology, University of Colorado Health Sciences Center, 4200 East Ninth Avenue, Denver, Colorado, 80262, USA
- Division of Cellular and Molecular Medicine and Howard Hughes Medical Institute, University of California at San Diego, School of Medicine, La Jolla, California, 92093, USA
- These authors contributed equally to this work
Correspondence to: Michael Overduin2 e-mail: michael.overduin@uchsc.edu
