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Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation

Tutkimustuotosvertaisarvioitu

Standard

Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation. / Manna, Moutusi; Javanainen, Matti; Martinez-Seara Monne, Hector; Gabius, Hans-Joachim; Rog, Tomasz; Vattulainen, Ilpo.

julkaisussa: Biochimica et Biophysica Acta: Biomembranes, Vuosikerta 1859, Nro 5, 01.05.2017, s. 870-878.

Tutkimustuotosvertaisarvioitu

Harvard

Manna, M, Javanainen, M, Martinez-Seara Monne, H, Gabius, H-J, Rog, T & Vattulainen, I 2017, 'Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation', Biochimica et Biophysica Acta: Biomembranes, Vuosikerta. 1859, Nro 5, Sivut 870-878. https://doi.org/10.1016/j.bbamem.2017.01.033

APA

Manna, M., Javanainen, M., Martinez-Seara Monne, H., Gabius, H-J., Rog, T., & Vattulainen, I. (2017). Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation. Biochimica et Biophysica Acta: Biomembranes, 1859(5), 870-878. https://doi.org/10.1016/j.bbamem.2017.01.033

Vancouver

Manna M, Javanainen M, Martinez-Seara Monne H, Gabius H-J, Rog T, Vattulainen I. Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation. Biochimica et Biophysica Acta: Biomembranes. 2017 touko 1;1859(5):870-878. https://doi.org/10.1016/j.bbamem.2017.01.033

Author

Manna, Moutusi ; Javanainen, Matti ; Martinez-Seara Monne, Hector ; Gabius, Hans-Joachim ; Rog, Tomasz ; Vattulainen, Ilpo. / Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation. Julkaisussa: Biochimica et Biophysica Acta: Biomembranes. 2017 ; Vuosikerta 1859, Nro 5. Sivut 870-878.

Bibtex - Lataa

@article{1e68ad6c0eff42bfbe63b3d3e5bda7d9,
title = "Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation",
abstract = "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.",
keywords = "cholesterol, computer simulations, Glycosphingolipid, membrane domain, membrane registry, molecular dynamics",
author = "Moutusi Manna and Matti Javanainen and {Martinez-Seara Monne}, Hector and Hans-Joachim Gabius and Tomasz Rog and Ilpo Vattulainen",
year = "2017",
month = "5",
day = "1",
doi = "10.1016/j.bbamem.2017.01.033",
language = "English",
volume = "1859",
pages = "870--878",
journal = "Biochimica et Biophysica Acta: Biomembranes",
issn = "0005-2736",
publisher = "Elsevier",
number = "5",

}

RIS (suitable for import to EndNote) - Lataa

TY - JOUR

T1 - Long-chain GM1 gangliosides alter transmembrane domain registration through interdigitation

AU - Manna, Moutusi

AU - Javanainen, Matti

AU - Martinez-Seara Monne, Hector

AU - Gabius, Hans-Joachim

AU - Rog, Tomasz

AU - Vattulainen, Ilpo

PY - 2017/5/1

Y1 - 2017/5/1

N2 - 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.

AB - 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.

KW - cholesterol

KW - computer simulations

KW - Glycosphingolipid

KW - membrane domain

KW - membrane registry

KW - molecular dynamics

U2 - 10.1016/j.bbamem.2017.01.033

DO - 10.1016/j.bbamem.2017.01.033

M3 - Article

VL - 1859

SP - 870

EP - 878

JO - Biochimica et Biophysica Acta: Biomembranes

JF - Biochimica et Biophysica Acta: Biomembranes

SN - 0005-2736

IS - 5

ER -