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FYVE fingers bind PtdIns(3)P

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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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Figure 1: The endosomal localization of EEA1-CT and its Hrs FYVE-finger hybrid depends on PI(3)K activity and an intact FYVE finger.
Figure 2: FYVE domains bind specifically to PtdIns(3)P in vitro.

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Authors and Affiliations

  1. Department of Biochemistry, The Norwegian Radium Hospital, N-0310, Oslo, Norway

    Jean-Michel Gaullier, Anne Simonsen & Harald Stenmark

  2. Department of Molecular Biology, University of Bergen, Bergen, N-5020, Norway

    Rein Aasland

Authors
  1. Jean-Michel Gaullier
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  2. Anne Simonsen
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  3. Antonello D'Arrigo
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  4. Bjørn Bremnes
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  5. Harald Stenmark
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  6. Rein Aasland
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Gaullier, JM., Simonsen, A., D'Arrigo, A. et al. FYVE fingers bind PtdIns(3)P. Nature 394, 432–433 (1998). https://doi.org/10.1038/28767

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