PX domain interaction with PtdIns3P targets Vam7 SNARE to vacuole membranes

Research output: Contribution to journalArticle

Authors

  • M Cheever
  • TK Sato
  • T de Beer
  • TG Kutateladze
  • SD Emr

Colleges, School and Institutes

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.

Details

Original languageEnglish
Pages (from-to)613-618
Number of pages6
JournalNature Cell Biology
Volume3
Publication statusPublished - 1 Jul 2001