Membrane curvature enables N-Ras lipid anchor sorting to liquid-ordered membrane phases
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Membrane curvature enables N-Ras lipid anchor sorting to liquid-ordered membrane phases. / Larsen, Jannik Bruun; Jensen, Martin Borch; Bhatia, Vikram Kjøller; Pedersen, Søren Ljungberg; Bjørnholm, Thomas; Iversen, Lars; Uline, Mark; Szleifer, Igal; Jensen, Knud Jørgen; Hatzakis, Nikos; Stamou, Dimitrios.
In: Nature Chemical Biology, Vol. 11, No. 3, 2015, p. 192-194.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Membrane curvature enables N-Ras lipid anchor sorting to liquid-ordered membrane phases
AU - Larsen, Jannik Bruun
AU - Jensen, Martin Borch
AU - Bhatia, Vikram Kjøller
AU - Pedersen, Søren Ljungberg
AU - Bjørnholm, Thomas
AU - Iversen, Lars
AU - Uline, Mark
AU - Szleifer, Igal
AU - Jensen, Knud Jørgen
AU - Hatzakis, Nikos
AU - Stamou, Dimitrios
PY - 2015
Y1 - 2015
N2 - Trafficking and sorting of membrane-anchored Ras GTPases are regulated by partitioning between distinct membrane domains. Here, in vitro experiments and microscopic molecular theory reveal membrane curvature as a new modulator of N-Ras lipid anchor and palmitoyl chain partitioning. Membrane curvature was essential for enrichment in raft-like liquid-ordered phases; enrichment was driven by relief of lateral pressure upon anchor insertion and most likely affects the localization of lipidated proteins in general.
AB - Trafficking and sorting of membrane-anchored Ras GTPases are regulated by partitioning between distinct membrane domains. Here, in vitro experiments and microscopic molecular theory reveal membrane curvature as a new modulator of N-Ras lipid anchor and palmitoyl chain partitioning. Membrane curvature was essential for enrichment in raft-like liquid-ordered phases; enrichment was driven by relief of lateral pressure upon anchor insertion and most likely affects the localization of lipidated proteins in general.
U2 - 10.1038/nchembio.1733
DO - 10.1038/nchembio.1733
M3 - Journal article
C2 - 25622090
VL - 11
SP - 192
EP - 194
JO - Nature Chemical Biology
JF - Nature Chemical Biology
SN - 1552-4450
IS - 3
ER -
ID: 131361806