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

Cheever, Matthew L., Sato, Trey K., de Beer, Tonny, Kutateladze, Tatiana G., Emr, Scott D., Overduin, Michael·2001·Nature Cell Biology
DOI 10.1038/35083000
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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.

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  • The PX domain of sorting nexins binds phosphatidylinositol phosphates.

    “The hallmark of this family is the presence of a phox (PX) homology domain, which has been shown to bind to phosphatidylinositol phosphates (PtdInsPs) (Cheever et al, 2001;Kanai et al, 2001;Xu et al, 2001).”

    From Sorting nexin 17 facilitates LRP recycling in the early endosome (2005) · cites this paper as Cheever et al, 2001

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Metadata

Authors
Cheever, M. L., Sato, T. K., de Beer, T., Kutateladze, T. G., Emr, S. D., & Overduin, M.
Venue
Nature Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2001-05-24
Volume
3
Issue
7
Pages
613-618
ISSN
  • 1465-7392
  • 1476-4679
DOI
10.1038/35083000
Cited by
341
References
2
Language
en
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