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Biochem J. 2004 May 1;379(Pt 3):527-32.

Cholesterol-dependent partitioning of PtdIns(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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1
Department of Biochemistry, McMaster University, Hamilton L8N 3Z5, ON, Canada. epand@mcmaster.ca

Abstract

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-TMR-labelled PtdIns(4,5) P2 in bilayers of 1-palmitoyl-2-oleoyl phosphatidylcholine containing 40 mol% cholesterol and 0.1 mol% BODIPY-PtdIns(4,5)2. Both fluorescence spectroscopy and total internal reflectance fluorescence microscopy revealed the cholesterol-dependent nature of PtdIns(4,5) P2-enriched membrane-domain formation.

PMID:
14989697
PMCID:
PMC1224132
DOI:
10.1042/BJ20040204
[Indexed for MEDLINE]
Free PMC Article
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