期刊
JOURNAL OF LIPID RESEARCH
卷 47, 期 7, 页码 1521-1525出版社
ELSEVIER
DOI: 10.1194/jlr.M600121-JLR200
关键词
PIP2; lipid domains; fluorescence; fluorescence resonance energy transfer
Phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P-2] 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)P-2 in plasma membrane domains. Here, we show that PI(4,5)P-2 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)P-2 to domains as a mechanism for the compartmentalization of PI(4,5)P-2 in the plasma membrane. Water/ bilayer partition of PI(4,5)P-2 is also shown to be dependent on the protonation state of the lipid.
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