Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
28143757
DOI
10.1016/j.bbamem.2017.01.033
PII: S0005-2736(17)30041-X
Knihovny.cz E-resources
- Keywords
- Glycosphingolipid, cholesterol, computer simulations, membrane domain, membrane registry, molecular dynamics,
- MeSH
- G(M1) Ganglioside chemistry MeSH
- Lipid Bilayers chemistry MeSH
- Molecular Dynamics Simulation MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- G(M1) Ganglioside MeSH
- Lipid Bilayers MeSH
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.
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