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The role of interfacial lipids in stabilizing membrane protein oligomers

Author

Listed:
  • Kallol Gupta

    (University of Oxford)

  • Joseph A. C. Donlan

    (University of Oxford)

  • Jonathan T. S. Hopper

    (University of Oxford)

  • Povilas Uzdavinys

    (Centre for Biomembrane Research, Stockholm University)

  • Michael Landreh

    (University of Oxford)

  • Weston B. Struwe

    (University of Oxford)

  • David Drew

    (Centre for Biomembrane Research, Stockholm University)

  • Andrew J. Baldwin

    (University of Oxford)

  • Phillip J. Stansfeld

    (University of Oxford)

  • Carol V. Robinson

    (University of Oxford)

Abstract

Membrane lipids such as cardiolipin act as molecular glue to preserve the oligomeric states of membrane proteins with low oligomeric stability.

Suggested Citation

  • Kallol Gupta & Joseph A. C. Donlan & Jonathan T. S. Hopper & Povilas Uzdavinys & Michael Landreh & Weston B. Struwe & David Drew & Andrew J. Baldwin & Phillip J. Stansfeld & Carol V. Robinson, 2017. "The role of interfacial lipids in stabilizing membrane protein oligomers," Nature, Nature, vol. 541(7637), pages 421-424, January.
    • Handle: RePEc:nat:nature:v:541:y:2017:i:7637:d:10.1038_nature20820
    DOI: 10.1038/nature20820
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    Cited by:

    1. Abraham O. Oluwole & Robin A. Corey & Chelsea M. Brown & Victor M. Hernández-Rocamora & Phillip J. Stansfeld & Waldemar Vollmer & Jani R. Bolla & Carol V. Robinson, 2022. "Peptidoglycan biosynthesis is driven by lipid transfer along enzyme-substrate affinity gradients," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Jixing Lyu & Chang Liu & Tianqi Zhang & Samantha Schrecke & Nicklaus P. Elam & Charles Packianathan & Georg K. A. Hochberg & David Russell & Minglei Zhao & Arthur Laganowsky, 2022. "Structural basis for lipid and copper regulation of the ABC transporter MsbA," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    3. Atsushi Yamagata & Yoshiko Murata & Kosuke Namba & Tohru Terada & Shuya Fukai & Mikako Shirouzu, 2022. "Uptake mechanism of iron-phytosiderophore from the soil based on the structure of yellow stripe transporter," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    4. Yongchan Lee & Pattama Wiriyasermkul & Pornparn Kongpracha & Satomi Moriyama & Deryck J. Mills & Werner Kühlbrandt & Shushi Nagamori, 2022. "Ca2+-mediated higher-order assembly of heterodimers in amino acid transport system b0,+ biogenesis and cystinuria," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    5. Ondřej Gahura & Alexander Mühleip & Carolina Hierro-Yap & Brian Panicucci & Minal Jain & David Hollaus & Martina Slapničková & Alena Zíková & Alexey Amunts, 2022. "An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    6. Vishal Maingi & Zhao Zhang & Chris Thachuk & Namita Sarraf & Edwin R. Chapman & Paul W. K. Rothemund, 2023. "Digital nanoreactors to control absolute stoichiometry and spatiotemporal behavior of DNA receptors within lipid bilayers," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    7. Iven Winkelmann & Povilas Uzdavinys & Ian M. Kenney & Joseph Brock & Pascal F. Meier & Lina-Marie Wagner & Florian Gabriel & Sukkyeong Jung & Rei Matsuoka & Christoph Ballmoos & Oliver Beckstein & Dav, 2022. "Crystal structure of the Na+/H+ antiporter NhaA at active pH reveals the mechanistic basis for pH sensing," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    8. Junke Liu & Hengmin Tang & Chanjuan Xu & Shengnan Zhou & Xunying Zhu & Yuanyuan Li & Laurent Prézeau & Tao Xu & Jean-Philippe Pin & Philippe Rondard & Wei Ji & Jianfeng Liu, 2022. "Biased signaling due to oligomerization of the G protein-coupled platelet-activating factor receptor," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    9. Di Wu & Renhong Yan & Siyuan Song & Andrew K. Swansiger & Yaning Li & James S. Prell & Qiang Zhou & Carol V. Robinson, 2024. "The complete assembly of human LAT1-4F2hc complex provides insights into its regulation, function and localisation," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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