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PMID: 14989697 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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).

The Biochemical journal ·Vol. 379 ·No. Pt 3 ·2004-05-01 ·Pages 527-32

Epand RM, Vuong P, Yip CM, Maekawa S, Epand RF

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.

MeSH Terms
Cholesterol/metabolism Fluorescence Hydrolysis Lipid Bilayers/chemistry,metabolism Membrane Microdomains/chemistry,metabolism Membrane Proteins Nerve Tissue Proteins/chemistry,metabolism Phosphatidylcholines/metabolism Phosphatidylinositol 4,5-Diphosphate Phosphatidylinositol Phosphates/metabolism Repressor Proteins/chemistry,metabolism Spectrometry, Fluorescence Type C Phospholipases/metabolism
Chemicals
BASP1 protein, human Lipid Bilayers Membrane Proteins Nerve Tissue Proteins Phosphatidylcholines Phosphatidylinositol 4,5-Diphosphate Phosphatidylinositol Phosphates Repressor Proteins Cholesterol Type C Phospholipases 1-palmitoyl-2-oleoylphosphatidylcholine
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Epand Richard M
Department of Biochemistry, McMaster University, Hamilton L8N 3Z5, ON, Canada. epand@mcmaster.ca
Vuong Phan
Yip Christopher M
Maekawa Shohei
Epand Raquel F
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
1470-8728
Published
2004-05-01
Pages
527-32
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1224132
Subset
IM
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