A functional PtdIns(3)P-binding motif

Varsha Patki, Deirdre C. Lawe, Silvia Corvera (), Joseph V. Virbasius and Anil Chawla
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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

Nature, 1998, vol. 394, issue 6692, 433-434

Abstract: 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.

Date: 1998
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DOI: 10.1038/28771

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