Počet záznamů: 1
Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation
- 1.
SYSNO ASEP 0475321 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation Tvůrce(i) Manna, M. (FI)
Javanainen, M. (FI)
Martinez-Seara Monne, Hector (UOCHB-X) ORCID, RID
Gabius, H. J. (DE)
Rog, T. (FI)
Vattulainen, I. (FI)Zdroj.dok. Biochimica Et Biophysica Acta-Biomembranes. - : Elsevier - ISSN 0005-2736
Roč. 1859, č. 5 (2017), s. 870-878Poč.str. 9 s. Jazyk dok. eng - angličtina Země vyd. NL - Nizozemsko Klíč. slova glycosphingolipid ; cholesterol ; membrane domain ; membrane registry ; molecular dynamics ; computer simulations Vědní obor RIV CF - Fyzikální chemie a teoretická chemie Obor OECD Physical chemistry Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000398870800022 EID SCOPUS 85012110513 DOI 10.1016/j.bbamem.2017.01.033 Anotace 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. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Rok sběru 2018
Počet záznamů: 1