Phosphoinositide 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.
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| Gene/Complex | Qualifier | Gene Ontology Term | Annotation Extension | Evidence | Source | Assigned On |
|---|---|---|---|---|---|---|
| PIB1 | enables | phosphatidylinositol-3-phosphate binding | IDA | SGD | 2013-08-07 | |
| PEP7 | enables | phosphatidylinositol-3-phosphate binding | IDA | SGD | 2013-08-07 | |
| FAB1 | enables | phosphatidylinositol-3-phosphate binding | IDA | SGD | 2013-08-07 | |
| VPS27 | enables | phosphatidylinositol-3-phosphate binding | IDA | SGD | 2013-08-07 |