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Journal of Cell Science, Vol 112, Issue 23 4175-4183, Copyright © 1999 by Company of Biologists
JOURNAL ARTICLES |
H Stenmark and R Aasland
Dept of Biochemistry, the Norwegian Radium Hospital, Montebello, N-0310 Oslo, Norway.
The 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.
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