Phox domain interaction with Ptdlns(3)P targets the Vam7 t-SNARE to vacuole membranes Academic Article uri icon

Overview

MeSH Major

  • Fungal Proteins
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Phosphatidylinositol Phosphates
  • Vesicular Transport Proteins

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.

publication date

  • July 20, 2001

Research

keywords

  • Academic Article

Identity

Language

  • eng

Digital Object Identifier (DOI)

  • 10.1038/35083000

PubMed ID

  • 11433291

Additional Document Info

start page

  • 613

end page

  • 8

volume

  • 3

number

  • 7