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A functional PtdIns(3)P-binding motif

Author

Listed:
  • Varsha Patki

    (University of Massachusetts Medical School)

  • Deirdre C. Lawe

    (University of Massachusetts Medical School)

  • Silvia Corvera

    (University of Massachusetts Medical School)

  • Joseph V. Virbasius

    (Biochemistry and Molecular Biology, University of Massachusetts Medical School)

  • Anil Chawla

    (Biochemistry and Molecular Biology, University of Massachusetts Medical School)

Abstract

Treating cells with the phosphatidylinositol-3-OH kinase (PI(3)K) inhibitor wortmannin causes the dissociation of the early-endosomal antigen EEA1 from early endosomes1. EEA1 from cytosolic extracts binds to liposomes containing phosphatidylinositol-3-phosphate (PtdIns(3)P), the major product of PI(3)K in yeast and mammalian cells1,2. Here we show that a RING zinc-finger domain at the carboxy terminus of EEA1, previously identified and named the ‘FYVE’ domain3, binds directly and specifically to PtdIns(3)P. This indicates that proteins containing this motif may be downstream effectors of PI(3)K in yeast and mammalian cells.

Suggested Citation

  • Varsha Patki & Deirdre C. Lawe & Silvia Corvera & Joseph V. Virbasius & Anil Chawla, 1998. "A functional PtdIns(3)P-binding motif," Nature, Nature, vol. 394(6692), pages 433-434, July.
    • Handle: RePEc:nat:nature:v:394:y:1998:i:6692:d:10.1038_28771
    DOI: 10.1038/28771
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