A functional PtdIns(3)P-binding motif (original) (raw)
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- Published: 30 July 1998
Nature volume 394, pages 433–434 (1998)Cite this article
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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.
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Authors and Affiliations
- Program in Molecular Medicine and Department of Cell Biology, University of Massachusetts Medical School, Worcester, 01605, Massachusetts, USA
Varsha Patki, Deirdre C. Lawe & Silvia Corvera - Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, 01605, Massachusetts, USA
Joseph V. Virbasius & Anil Chawla
Authors
- Varsha Patki
You can also search for this author inPubMed Google Scholar - Deirdre C. Lawe
You can also search for this author inPubMed Google Scholar - Silvia Corvera
You can also search for this author inPubMed Google Scholar - Joseph V. Virbasius
You can also search for this author inPubMed Google Scholar - Anil Chawla
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Patki, V., Lawe, D., Corvera, S. et al. A functional PtdIns(3)P-binding motif.Nature 394, 433–434 (1998). https://doi.org/10.1038/28771
- Issue Date: 30 July 1998
- DOI: https://doi.org/10.1038/28771