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Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation

M. Manna, M. Javanainen, HM. Monne, HJ. Gabius, T. Rog, I. Vattulainen,

. 2017 ; 1859 (5) : 870-878. [pub] 20170128

Jazyk angličtina Země Nizozemsko

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc17031076

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.

Citace poskytuje Crossref.org

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$a Extracellular and cytosolic leaflets in cellular membranes are distinctly different in lipid composition, yet they contribute together to signaling across the membranes. Here we consider a mechanism based on long-chain gangliosides for coupling the extracellular and cytosolic membrane leaflets together. Based on atomistic molecular dynamics simulations, we find that long-chain GM1 in the extracellular leaflet exhibits a strong tendency to protrude into the opposing bilayer leaflet. This interdigitation modulates the order in the cytosolic monolayer and thereby strengthens the interaction and coupling across a membrane. Coarse-grained simulations probing longer time scales in large membrane systems indicate that GM1 in the extracellular leaflet modulates the phase behavior in the cytosolic monolayer. While short-chain GM1 maintains phase-symmetric bilayers with a strong membrane registration effect, the situation is altered with long-chain GM1. Here, the significant interdigitation induced by long-chain GM1 modulates the behavior in the cytosolic GM1-free leaflet, weakening and slowing down the membrane registration process. The observed physical interaction mechanism provides a possible means to mediate or foster transmembrane communication associated with signal transduction.
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$a Javanainen, Matti $u Department of Physics, Tampere University of Technology, P. O. Box 692, FI- 33101 Tampere, Finland; Department of Physics, POB 64, FI-00014 University of Helsinki, Finland.
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$a Monne, Hector Martinez-Seara $u Department of Physics, Tampere University of Technology, P. O. Box 692, FI- 33101 Tampere, Finland; Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, CZ-16610, Prague, Czech Republic.
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$a Gabius, Hans-Joachim $u Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig Maximilian University, D-80539 Munchen, Germany.
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$a Rog, Tomasz $u Department of Physics, Tampere University of Technology, P. O. Box 692, FI- 33101 Tampere, Finland; Department of Physics, POB 64, FI-00014 University of Helsinki, Finland.
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$a Vattulainen, Ilpo $u Department of Physics, Tampere University of Technology, P. O. Box 692, FI- 33101 Tampere, Finland; Department of Physics, POB 64, FI-00014 University of Helsinki, Finland; MEMPHYS-Center for Biomembrane Physics, University of Southern Denmark, Odense, Denmark. Electronic address: Ilpo.Vattulainen@helsinki.fi.
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