Identification of a phosphatidylinositol‐4,5‐bisphosphate‐binding domain in the N‐terminal region of ezrin

FEBS Letters

Andréoli, Christophe¹  Roy, Christian¹  Mangeat, Paul¹  Niggli, Verena² 

[1] Dynamique Moléculaire des Interactions Membranaires, CNRS URA 1856, Université Montpellier II, 34095 Montpellier Cedex 5, France;Department of Pathology, University of Bern, Murtenstr. 31, 3010-Bern, Switzerland

关键词: Ezrin;    Phosphatidylinositol-4;    5-bisphosphate;    Acidic phospholipid;    Lipid interaction;    GST;    glutathione S-transferase;    PC;    phosphatidyl-choline;    PIP2;    phospatidyl-inositol-4;    5-bisphosphate;    PIP;    phosphatidylinositol-4-monophosphate;    PI;    phosphatidyl-inositol;    PS;    phosphatidylserine;   

DOI  :  10.1016/0014-5793(95)01270-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 (PIP₂), the residual being phosphatidylcholine (PC). When PIP₂ 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 PIP₂-containing liposomes, whereas a C-terminal fusion protein (310–586) has lost this ability.

【 授权许可】

Unknown