Scientific Correspondence | Published:

FYVE fingers bind PtdIns(3)P

Nature volume 394, pages 432433 (30 July 1998) | Download Citation

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Abstract

The membrane lipid phosphatidylinositol-3-phosphate (PtdIns(3)P) is constitutively produced by yeast and higher eukaryotes through the phosphorylation of phosphatidylinositol by phosphatidylinositol-3-OH kinase1 (PI(3)K). PtdIns(3)P is important for vesicular transport1, but little is known about how it acts, and proteins that specifically recognize it have not yet been identified. Here we identify the FYVE finger2, an evolutionarily conserved double-zinc-binding domain (see Supplementary information), as a protein structure that binds to PtdIns(3)P with high specificity.

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Author information

Affiliations

  1. Department of Biochemistry, The Norwegian Radium Hospital, N-0310 Oslo, Norway  e-mail: stenmark@ulrik.uio.no

    • Jean-Michel Gaullier
    • , Anne Simonsen
    •  & Harald Stenmark
  2. Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway

    • Rein Aasland

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DOI

https://doi.org/10.1038/28767

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