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Identification of a phosphatidylinositol‐4,5‐bisphosphate‐binding domain in the N‐terminal region of ezrin
Author(s) -
Niggli Verena,
Andréoli Christophe,
Roy Christian,
Mangeat Paul
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01270-1
Subject(s) - phosphatidylinositol , liposome , ezrin , phosphatidylserine , chemistry , fusion protein , recombinant dna , biochemistry , phosphatidylinositol 4,5 bisphosphate , biophysics , microbiology and biotechnology , phospholipid , biology , kinase , cytoskeleton , membrane , gene , cell
Purified human recombinant ezrin cosediments with large liposomes containing phosphatidylserine (PS). This interaction is optimal at low ionic strength. At physiological ionic strength (130 mM KCl) ezrin interacts strongly with liposomes containing ≥5% phosphatidylinositol‐4,5‐bisphosphate (PIP 2 ), the residual being phosphatidylcholine (PC). When PIP 2 is replaced by phosphatidylinositol‐4‐monophosphate (PIP), phosphatidylinositol (PI) or PS, the interaction is markedly reduced. Furthermore we show, that a purified N‐terminal glutathione S ‐transferase (GST) fusion protein of ezrin (1–309) still has retained the capacity to interact with PIP 2 ‐containing liposomes, whereas a C‐terminal fusion protein (310–586) has lost this ability.