Structure and Origin of Ordered Lipid Domains in Biological Membranes

Structure and Origin of Ordered Lipid Domains in Biological Membranes J. Membrane Biol. 164, 103–114 (1998) The Journal of Membrane Biology © Springer-Verlag New York Inc. 1998 Topical Review D.A. Brown, E. London Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York at Stony Brook, Stony Brook, NY 11794-5215, USA Received: 26 January 1998/Revised: 9 March 1998 Introduction recent reviews of DRMs and the ordered-domain model [5, 6], and to two other insightful reviews of these do- mains [8, 82]. The clearest function of membrane lipids is to form am- Increasing evidence suggests that another type of phipathic bilayers that surround cells and organelles and domain, formed by electrostatic interactions between block leakage of hydrophilic compounds while housing membrane-associated components, may exist in mem- membrane proteins. However, the wide variety of lipids branes [44]. One intriguing example is the ability of a observed in biological membranes would not be required membrane-associated positively charged peptide derived for a simple barrier function. Phospholipids alone dis- from the MARCKS protein to organize domains rich in play a variety of headgroup and acyl chain structures, phosphatidylinositol bisphosphate [19]. Though poten- and eukaryotic cell membranes often contain sphingolip- tially very important, formation of these domains will http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Structure and Origin of Ordered Lipid Domains in Biological Membranes

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Publisher
Springer Journals
Copyright
Copyright © Inc. by 1998 Springer-Verlag New York
Subject
Life Sciences; Biochemistry, general; Human Physiology
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s002329900397
Publisher site
See Article on Publisher Site

Abstract

J. Membrane Biol. 164, 103–114 (1998) The Journal of Membrane Biology © Springer-Verlag New York Inc. 1998 Topical Review D.A. Brown, E. London Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York at Stony Brook, Stony Brook, NY 11794-5215, USA Received: 26 January 1998/Revised: 9 March 1998 Introduction recent reviews of DRMs and the ordered-domain model [5, 6], and to two other insightful reviews of these do- mains [8, 82]. The clearest function of membrane lipids is to form am- Increasing evidence suggests that another type of phipathic bilayers that surround cells and organelles and domain, formed by electrostatic interactions between block leakage of hydrophilic compounds while housing membrane-associated components, may exist in mem- membrane proteins. However, the wide variety of lipids branes [44]. One intriguing example is the ability of a observed in biological membranes would not be required membrane-associated positively charged peptide derived for a simple barrier function. Phospholipids alone dis- from the MARCKS protein to organize domains rich in play a variety of headgroup and acyl chain structures, phosphatidylinositol bisphosphate [19]. Though poten- and eukaryotic cell membranes often contain sphingolip- tially very important, formation of these domains will

Journal

The Journal of Membrane BiologySpringer Journals

Published: Jul 15, 1998

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