Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation

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http://hdl.handle.net/10138/232319

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Manna , M , Javanainen , M , Monne , H M-S , Gabius , H-J , Rog , T & Vattulainen , I 2017 , ' Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation ' , Biochimica et Biophysica Acta. Biomembranes , vol. 1859 , no. 5 , pp. 870-878 . https://doi.org/10.1016/j.bbamem.2017.01.033

Title: Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation
Author: Manna, Moutusi; Javanainen, Matti; Monne, Hector Martinez-Seara; Gabius, Hans-Joachim; Rog, Tomasz; Vattulainen, Ilpo
Other contributor: University of Helsinki, Department of Physics
University of Helsinki, Department of Physics
University of Helsinki, Department of Physics
Date: 2017-05
Language: eng
Number of pages: 9
Belongs to series: Biochimica et Biophysica Acta. Biomembranes
ISSN: 0005-2736
DOI: https://doi.org/10.1016/j.bbamem.2017.01.033
URI: http://hdl.handle.net/10138/232319
Abstract: Extracellular and cytosolic leaflets in cellular membranes are distinctly different in lipid composition, yet they contribute together to signaling across the membranes. Here we consider a mechanism based on long-chain gangliosides for coupling the extracellular and cytosolic membrane leaflets together. Based on atomistic molecular dynamics simulations, we find that long-chain GM1 in the extracellular leaflet exhibits a strong tendency to protrude into the opposing bilayer leaflet. This interdigitation modulates the order in the cytosolic monolayer and thereby strengthens the interaction and coupling across a membrane. Coarse-grained simulations probing longer time scales in large membrane systems indicate that GM1 in the extracellular leaflet modulates the phase behavior in the cytosolic monolayer. While short-chain GM1 maintains phase-symmetric bilayers with a strong membrane registration effect, the situation is altered with long-chain GM1. Here, the significant interdigitation induced by long-chain GM1 modulates the behavior in the cytosolic GM1-free leaflet, weakening and slowing down the membrane registration process. The observed physical interaction mechanism provides a possible means to mediate or foster transmembrane communication associated with signal transduction. (C) 2017 Elsevier B.V. All rights reserved.
Subject: Glycosphingolipid
cholesterol
membrane domain
membrane registry
molecular dynamics
computer simulations
ATOM FORCE-FIELD
MOLECULAR-DYNAMICS SIMULATIONS
ENTEROCYTE-LIKE CELLS
FATTY-ACID CONTENT
MODEL MEMBRANES
LIPID-BILAYERS
NEUROBLASTOMA-CELLS
ASYMMETRIC BILAYERS
PHASE-SEPARATION
PLASMA-MEMBRANE
114 Physical sciences
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