IDENTIFICATION OF A PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE-BINDING DOMAIN IN THE N-TERMINAL REGION OF EZRIN
IDENTIFICATION OF A PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE-BINDING DOMAIN IN THE N-TERMINAL REGION OF EZRIN
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DOI：
10.1016/0014-5793(95)01270-1
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发表时间：
1995-12-04
期刊：
影响因子：
3.5
通讯作者：
MANGEAT, P
中科院分区：
文献类型：
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作者：
NIGGLI, V;ANDREOLI, C;MANGEAT, P
纯化的人重组埃兹蛋白辅料与含有磷脂酰丝氨酸 (PS) 的大脂质体。这种相互作用在低离子强度下是最佳的。在生理离子强度 (130 mM KCI) 下，埃兹蛋白与含有大于或等于 5% 磷脂酰肌醇-4,5-二磷酸 (PIP2) 的脂质体强烈相互作用，残留物为磷脂酰胆碱 (PC)。当 PIP2 被 4-单磷酸磷脂酰肌醇 (PIP)、磷脂酰肌醇 (PI) 或 PS 取代时，相互作用显着降低。此外，我们还发现，纯化的 ezrin (1-309) N 端谷胱甘肽 S 转移酶 (GST) 融合蛋白仍然保留了与含有 PIP2 的脂质体相互作用的能力，而 C 端融合蛋白 (310-586) 则失去了这种能力。
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 KCI) ezrin interacts strongly with liposomes containing greater than or equal to 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.