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Nat Cell Biol. 2001 Jul;3(7):613-8.

Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.

Author information

1
Molecular Biology Program, University of Colorado Health Sciences Center, 4200 East Ninth Avenue, Denver, Colorado 80262, USA.

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.

PMID:
11433291
DOI:
10.1038/35083000
[Indexed for MEDLINE]

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