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lüll FYVE-finger proteins--effectors of an inositol lipid Stenmark H; Aasland RJ Cell Sci 1999[Dec]; 112 ( Pt 23) (ä): 4175-83The binding of cytosolic proteins to specific intracellular membranes containing phosphorylated derivatives of phosphatidylinositol (PtdIns) is a common theme in vital cellular processes, such as cytoskeletal function, receptor signalling and membrane trafficking. Recently, several potential effectors of the phosphoinositide 3-kinase product PtdIns 3-phosphate (PtdIns(3)P) have emerged through the observation that a conserved zinc-finger-like domain, the FYVE-finger, binds specifically to this lipid. Here we review current knowledge about the structural basis for the FYVE-PtdIns(3)P interaction, its role in membrane recruitment of proteins and the functions of FYVE-finger proteins in membrane trafficking and other cellular processes.|*Zinc Fingers[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Consensus Sequence[MESH]|Conserved Sequence[MESH]|Humans[MESH]|Molecular Sequence Data[MESH]|Phosphatidylinositol 3-Kinases/*metabolism[MESH]|Phosphatidylinositol Phosphates/*metabolism[MESH]|Phosphorylation[MESH]|Protein Conformation[MESH]|Protein Structure, Secondary[MESH]|Proteins/*chemistry/genetics/metabolism[MESH]|Sequence Alignment[MESH]|Sequence Homology, Amino Acid[MESH] |