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File:Phosphatidylinositol Phosphate.jpg
Names
Other names PIP, PI(4)P
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). Infobox references

Phosphatidylinositol phosphate (PIP) is a glycerophospholipid. PIP is produced from the phosphorylation of PI, which primarily forms PI(3)P and PI(4)P. Specifically, Phosphoinositide 3-kinase produces PI(3)P from Phosphatidylinositol.

Similar to other phosphatidylinositols, PIP also exhibits polymorphic behaviour.

PI(3)P Binding Module

Several studies have identified a PI(3)P binding module, the FYVE domain. The FYVE domain is named after the cysteine-rich proteins, Fab1p, YOTB, Vac1p, and early endosome antigen 1 (EEA1), and has been connected to vacuolar protein sorting and endosome function. . The proteins are characterized by having basic amino acids around the cysteines, and are able to coordinate with Zinc atoms. The metal coordination and basic amino acids are required for the acidic head group of PI(3)P to bind to the FYVE domain. It has been speculated these bindings cause conformational changes or regulate protein-protein or lipid-protein interactions.

References

1. Leevers SJ, Vanhaesebroeck B, Waterfield MD (April 1999). "Signalling through phosphoinositide 3-kinases: the lipids take centre stage". Current Opinion in Cell Biology 11 (2): 219–25. doi:10.1016/S0955-0674(99)80029-5. PMID 10209156.

2. Corvera, S.; Czech, MP. Direct Targets of Phosphoinositide 3-Kinase Products in Membrane Traffic and Signal Transduction. Trends in Cell Biology. 1998 8:442-446.

3. Wiedemann, C.; Cockcroft, S. Sticky Fingers Grab a Lipid. Nature 1998 394:426-427.

• J. M. Seddon, R. H. Templer. Polymorphism of Lipid-Water Systems, from the Handbook of Biological Physics, Vol. 1, ed. R. Lipowsky, and E. Sackmann. (c) 1995 Elsevier Science B.V. ISBN 0-444-81975-4
• X. Mulet, Ph.D. thesis, Imperial College, University of London, 2005.