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Journal of Lipid Research, Vol. 47, 1521-1525, July 2006
Copyright © 2006 by American Society for Biochemistry and Molecular Biology

Absence of clustering of phosphatidylinositol-(4,5)-bisphosphate in fluid phosphatidylcholine

Fábio Fernandes^1,*, Luís M. S. Loura^*,, Alexander Fedorov^* and Manuel Prieto^*

^* Centro de Química-Física Molecular, Instituto Superior Técnico, Lisbon, Portugal
Centro de Química e Departamento de Química, Universidade de Évora, Évora, Portugal

Published, JLR Papers in Press, April 21, 2006.

¹ To whom correspondence should be addressed. e-mail: fernandesf{at}ist.utl.pt

Phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P₂] plays a key role in the modulation of actin polymerization and vesicle trafficking. These processes seem to depend on the enrichment of PI(4,5)P₂ in plasma membrane domains. Here, we show that PI(4,5)P₂ does not form domains when in a fluid phosphatidylcholine matrix in the pH range of 4.8–8.4. This finding is at variance with the spontaneous segregation of PI(4,5)P₂ to domains as a mechanism for the compartmentalization of PI(4,5)P₂ in the plasma membrane. Water/bilayer partition of PI(4,5)P₂ is also shown to be dependent on the protonation state of the lipid.

Abbreviations: DPH, diphenylhexatriene; DPPC, 1,2-dipalmitoylphosphatidycholine; FRET, fluorescence resonance energy transfer; NBD, 7-nitro-2-1,3-benzoxadiazol; PC, phosphatidylcholine; PI(4,5)P₂, phosphatidylinositol-(4,5)-bisphosphate; POPG, 1-palmitoyl-2-oleoylphosphatidylglycerol

Supplementary key words PIP2 • lipid domains • fluorescence • fluorescence resonance energy transfer

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