How curved membranes recruit amphipathic helices and protein anchoring motifs

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How curved membranes recruit amphipathic helices and protein anchoring motifs. / Hatzakis, Nikos; Bhatia, Vikram Kjøller; Larsen, Jannik; Madsen, Kenneth Lindegaard; Bolinger, Pierre-Yves; Kunding, Andreas Hjarne; Castillo Leon, John Jairo; Gether, Ulrik; Hedegård, Per; Stamou, Dimitrios.

In: Nature Chemical Biology, Vol. 5, No. 11, 2009, p. 835-841.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Hatzakis, N, Bhatia, VK, Larsen, J, Madsen, KL, Bolinger, P-Y, Kunding, AH, Castillo Leon, JJ, Gether, U, Hedegård, P & Stamou, D 2009, 'How curved membranes recruit amphipathic helices and protein anchoring motifs' Nature Chemical Biology, vol. 5, no. 11, pp. 835-841. https://doi.org/10.1038/nchembio.213

APA

Hatzakis, N., Bhatia, V. K., Larsen, J., Madsen, K. L., Bolinger, P-Y., Kunding, A. H., ... Stamou, D. (2009). How curved membranes recruit amphipathic helices and protein anchoring motifs. Nature Chemical Biology, 5(11), 835-841. https://doi.org/10.1038/nchembio.213

Vancouver

Hatzakis N, Bhatia VK, Larsen J, Madsen KL, Bolinger P-Y, Kunding AH et al. How curved membranes recruit amphipathic helices and protein anchoring motifs. Nature Chemical Biology. 2009;5(11):835-841. https://doi.org/10.1038/nchembio.213

Author

Hatzakis, Nikos ; Bhatia, Vikram Kjøller ; Larsen, Jannik ; Madsen, Kenneth Lindegaard ; Bolinger, Pierre-Yves ; Kunding, Andreas Hjarne ; Castillo Leon, John Jairo ; Gether, Ulrik ; Hedegård, Per ; Stamou, Dimitrios. / How curved membranes recruit amphipathic helices and protein anchoring motifs. In: Nature Chemical Biology. 2009 ; Vol. 5, No. 11. pp. 835-841.

Bibtex

@article{1314a380b0f511df825b000ea68e967b,
title = "How curved membranes recruit amphipathic helices and protein anchoring motifs",
abstract = "Lipids and several specialized proteins are thought to be able to sense the curvature of membranes (MC). Here we used quantitative fluorescence microscopy to measure curvature-selective binding of amphipathic motifs on single liposomes 50-700 nm in diameter. Our results revealed that sensing is predominantly mediated by a higher density of binding sites on curved membranes instead of higher affinity. We proposed a model based on curvature-induced defects in lipid packing that related these findings to lipid sorting and accurately predicted the existence of a new ubiquitous class of curvature sensors: membrane-anchored proteins. The fact that unrelated structural motifs such as alpha-helices and alkyl chains sense MC led us to propose that MC sensing is a generic property of curved membranes rather than a property of the anchoring molecules. We therefore anticipate that MC will promote the redistribution of proteins that are anchored in membranes through other types of hydrophobic moieties.",
author = "Nikos Hatzakis and Bhatia, {Vikram Kj{\o}ller} and Jannik Larsen and Madsen, {Kenneth Lindegaard} and Pierre-Yves Bolinger and Kunding, {Andreas Hjarne} and {Castillo Leon}, {John Jairo} and Ulrik Gether and Per Hedeg{\aa}rd and Dimitrios Stamou",
note = "Keywords: Biotinylation; Fluoresceins; Kinetics; Lipid Bilayers; Liposomes; Membrane Lipids; Membrane Proteins; Membranes; Microscopy, Confocal; Microscopy, Fluorescence; Models, Molecular; Peptides",
year = "2009",
doi = "10.1038/nchembio.213",
language = "English",
volume = "5",
pages = "835--841",
journal = "Nature Chemical Biology",
issn = "1552-4450",
publisher = "nature publishing group",
number = "11",

}

RIS

TY - JOUR

T1 - How curved membranes recruit amphipathic helices and protein anchoring motifs

AU - Hatzakis, Nikos

AU - Bhatia, Vikram Kjøller

AU - Larsen, Jannik

AU - Madsen, Kenneth Lindegaard

AU - Bolinger, Pierre-Yves

AU - Kunding, Andreas Hjarne

AU - Castillo Leon, John Jairo

AU - Gether, Ulrik

AU - Hedegård, Per

AU - Stamou, Dimitrios

N1 - Keywords: Biotinylation; Fluoresceins; Kinetics; Lipid Bilayers; Liposomes; Membrane Lipids; Membrane Proteins; Membranes; Microscopy, Confocal; Microscopy, Fluorescence; Models, Molecular; Peptides

PY - 2009

Y1 - 2009

N2 - Lipids and several specialized proteins are thought to be able to sense the curvature of membranes (MC). Here we used quantitative fluorescence microscopy to measure curvature-selective binding of amphipathic motifs on single liposomes 50-700 nm in diameter. Our results revealed that sensing is predominantly mediated by a higher density of binding sites on curved membranes instead of higher affinity. We proposed a model based on curvature-induced defects in lipid packing that related these findings to lipid sorting and accurately predicted the existence of a new ubiquitous class of curvature sensors: membrane-anchored proteins. The fact that unrelated structural motifs such as alpha-helices and alkyl chains sense MC led us to propose that MC sensing is a generic property of curved membranes rather than a property of the anchoring molecules. We therefore anticipate that MC will promote the redistribution of proteins that are anchored in membranes through other types of hydrophobic moieties.

AB - Lipids and several specialized proteins are thought to be able to sense the curvature of membranes (MC). Here we used quantitative fluorescence microscopy to measure curvature-selective binding of amphipathic motifs on single liposomes 50-700 nm in diameter. Our results revealed that sensing is predominantly mediated by a higher density of binding sites on curved membranes instead of higher affinity. We proposed a model based on curvature-induced defects in lipid packing that related these findings to lipid sorting and accurately predicted the existence of a new ubiquitous class of curvature sensors: membrane-anchored proteins. The fact that unrelated structural motifs such as alpha-helices and alkyl chains sense MC led us to propose that MC sensing is a generic property of curved membranes rather than a property of the anchoring molecules. We therefore anticipate that MC will promote the redistribution of proteins that are anchored in membranes through other types of hydrophobic moieties.

U2 - 10.1038/nchembio.213

DO - 10.1038/nchembio.213

M3 - Journal article

VL - 5

SP - 835

EP - 841

JO - Nature Chemical Biology

JF - Nature Chemical Biology

SN - 1552-4450

IS - 11

ER -

ID: 21593748