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)

被引:35
作者
Epand, RM [1 ]
Vuong, P
Yip, CM
Maekawa, S
Epand, RF
机构
[1] McMaster Univ, Dept Biochem, Hamilton, ON L8N 3Z5, Canada
[2] Univ Toronto, Inst Biomat & Biomed Engn, Dept Chem Engn & Appl Chem, Toronto, ON M5S 3G9, Canada
[3] Kobe Univ, Grad Sch Sci & Technol, Dept Life Sci, Dept Bioinformat,Nada Ku, Kobe, Hyogo 6578501, Japan
关键词
cholesterol; fluorescence; membrane raft; neuronal axonal myristoylated membrane protein of 22 kDa (NAP-22); Ptdlns(4,5)P2; total internal reflectance fluorescence (TIRF) microscopy;
D O I
10.1042/BJ20040204
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:527 / 532
页数:6
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