Počet záznamů: 1  

Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation

  1. 1. 0475321 - UOCHB-X 2018 RIV NL eng J - Článek v odborném periodiku
    Manna, M. - Javanainen, M. - Martinez-Seara Monne, Hector - Gabius, H. J. - Rog, T. - Vattulainen, I.
    Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation.
    Biochimica Et Biophysica Acta-Biomembranes. Roč. 1859, č. 5 (2017), s. 870-878 ISSN 0005-2736
    Institucionální podpora: RVO:61388963
    Klíčová slova: glycosphingolipid * cholesterol * membrane domain * membrane registry * molecular dynamics * computer simulations
    Kód oboru RIV: CF - Fyzikální chemie a teoretická chemie
    Obor OECD: Physical chemistry
    Impakt faktor: 3.438, rok: 2017

    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.
    Trvalý link: http://hdl.handle.net/11104/0272153