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pubmed-article:9702203pubmed:abstractTextPhosphoinositide 3-kinases (PI(3)K) are important regulators of receptor signaling cascades and intracellular membrane trafficking. To date, no protein domain has been identified that binds specifically to Ptdlns(3)P and thereby recruits/activates downstream effectors of Ptdlns(3)P signaling. Using an in vivo assay in yeast that detects Vps34 PI(3)K-dependent intracellular localization of a GFP reporter protein, and in vitro lipid-binding assays, we demonstrate that cysteine-rich RING domains of the FYVE finger subfamily bind specifically to Ptdlns phosphorylated exclusively at the D-3 position of the inositol ring. GFP-FYVE domain fusion proteins localized predominantly to membranes of endocytic compartments and required active Vps34 PI(3)K. Our data establish a molecular link between Vps34 PI(3)K and several FYVE domain-containing proteins (Vac1p, Vps27p) required for vacuolar/lysosomal protein trafficking.lld:pubmed
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pubmed-article:9702203pubmed:dateRevised2010-11-18lld:pubmed
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pubmed-article:9702203pubmed:articleTitlePhosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains.lld:pubmed
pubmed-article:9702203pubmed:affiliationHoward Hughes Medical Institute, University of California, San Diego School of Medicine, La Jolla 92093-0668, USA.lld:pubmed
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pubmed-article:9702203pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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