Cholesterol-dependent partitioning of Ptdlns(4,5)P2 into membrane domains by the N-terminal fragment of NAP-22 (neuronal axonal myristoylated membrane protein of 22 kDa)
Cholesterol-dependent partitioning of Ptdlns(4,5)P2 into membrane domains by the N-terminal fragment of NAP-22 (neuronal axonal myristoylated membrane protein of 22 kDa)
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DOI：
10.1042/bj20040204
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发表时间：
2004-05-01
影响因子：
4.1
通讯作者：
Epand, RF
中科院分区：
文献类型：
--
作者：
Epand, RM;Vuong, P;Epand, RF
在含有40 mol %胆固醇和0.1 mol % BODIPY（R）-PtdIns（4，5）（2）的1-棕榈酰-2-油酰磷脂酰胆碱双层中，对应于NAP-22（22 kDa的神经元轴突肉豆蔻酰化膜蛋白）N-末端的肉豆蔻酰化肽导致BODIPY（R）-TMR标记的PtdIns（4，5）P-2的荧光淬灭。荧光光谱和全内反射荧光显微镜显示胆固醇依赖的性质PtdIns（4，5）P-2-丰富的膜结构域的形成。
A myristoylated peptide corresponding to the N-terminus of NAP-22 (neuronal axonal myristoylated membrane protein of 22 kDa) causes the quenching of the fluorescence of BODIPY(R)-TMR-labelled PtdIns(4,5)P-2 in bilayers of 1-palmitoyl-2-oleoyl phosphatidylcholine containing 40 mol % cholesterol and 0.1 mol % BODIPY(R)-Ptdlns(4,5)(2). Both fluorescence spectroscopy and total internal reflectance fluorescence microscopy revealed the cholesterol-dependent nature of PtdIns(4,5)P-2-enriched membrane-domain formation.