FYVE fingers bind PtdIns(3)P
Jean-Michel Gaullier,
Anne Simonsen,
Antonello D'Arrigo,
Bjørn Bremnes,
Harald Stenmark () and
Rein Aasland
Additional contact information
Jean-Michel Gaullier: The Norwegian Radium Hospital
Anne Simonsen: The Norwegian Radium Hospital
Harald Stenmark: The Norwegian Radium Hospital
Rein Aasland: University of Bergen
Nature, 1998, vol. 394, issue 6692, 432-433
Abstract:
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.
Date: 1998
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Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:394:y:1998:i:6692:d:10.1038_28767
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DOI: 10.1038/28767
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