PX domain interaction with PtdIns3P targets Vam7 SNARE to vacuole membranes

M Cheever, TK Sato, T de Beer, TG Kutateladze, SD Emr, Michael Overduin

    Research output: Contribution to journalArticle

    300 Citations (Scopus)


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


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