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Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00475321" target="_blank" >RIV/61388963:_____/17:00475321 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.bbamem.2017.01.033" target="_blank" >http://dx.doi.org/10.1016/j.bbamem.2017.01.033</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.bbamem.2017.01.033" target="_blank" >10.1016/j.bbamem.2017.01.033</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10403 - Physical chemistry

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2017

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Biochimica Et Biophysica Acta-Biomembranes

  • ISSN

    0005-2736

  • e-ISSN

  • Volume of the periodical

    1859

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    9

  • Pages from-to

    870-878

  • UT code for WoS article

    000398870800022

  • EID of the result in the Scopus database

    2-s2.0-85012110513