IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v479y2011i7374d10.1038_nature10545.html
   My bibliography  Save this article

Membrane protein sequestering by ionic protein–lipid interactions

Author

Listed:
  • Geert van den Bogaart

    (Max Planck Institute for Biophysical Chemistry, Am Faßberg 11)

  • Karsten Meyenberg

    (Institute for Organic and Biomolecular Chemistry, Georg-August-University Göttingen, Tammannstraße 2)

  • H. Jelger Risselada

    (Max Planck Institute for Biophysical Chemistry, Am Faßberg 11)

  • Hayder Amin

    (Max Planck Institute for Biophysical Chemistry, Am Faßberg 11)

  • Katrin I. Willig

    (Max Planck Institute for Biophysical Chemistry, Am Faßberg 11)

  • Barbara E. Hubrich

    (Institute for Organic and Biomolecular Chemistry, Georg-August-University Göttingen, Tammannstraße 2)

  • Markus Dier

    (Max Planck Institute for Biophysical Chemistry, Am Faßberg 11)

  • Stefan W. Hell

    (Max Planck Institute for Biophysical Chemistry, Am Faßberg 11)

  • Helmut Grubmüller

    (Max Planck Institute for Biophysical Chemistry, Am Faßberg 11)

  • Ulf Diederichsen

    (Institute for Organic and Biomolecular Chemistry, Georg-August-University Göttingen, Tammannstraße 2)

  • Reinhard Jahn

    (Max Planck Institute for Biophysical Chemistry, Am Faßberg 11)

Abstract

Electrostatic factors in membrane organization Exocytosis in neuronal cells requires the SNARE protein syntaxin-1A, which is clustered at sites where synaptic vesicles are poised to undergo exocytosis. Reinhard Jahn and colleagues use super-resolution stimulated-emission depletion (STED) microscopy to show that syntaxin clusters in the membrane through electrostatic interactions with the strongly anionic lipid phosphatidylinositol-4,5-bisphosphate (PIP2) into 70-nanometre microdomains. The results demonstrate that electrostatic protein–lipid interactions can result in the formation of microdomains independent of cholesterol or lipid phases and have important implications for the organization of the plasma membrane.

Suggested Citation

  • Geert van den Bogaart & Karsten Meyenberg & H. Jelger Risselada & Hayder Amin & Katrin I. Willig & Barbara E. Hubrich & Markus Dier & Stefan W. Hell & Helmut Grubmüller & Ulf Diederichsen & Reinhard J, 2011. "Membrane protein sequestering by ionic protein–lipid interactions," Nature, Nature, vol. 479(7374), pages 552-555, November.
  • Handle: RePEc:nat:nature:v:479:y:2011:i:7374:d:10.1038_nature10545
    DOI: 10.1038/nature10545
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature10545
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/nature10545?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Heidi Koldsø & David Shorthouse & Jean Hélie & Mark S P Sansom, 2014. "Lipid Clustering Correlates with Membrane Curvature as Revealed by Molecular Simulations of Complex Lipid Bilayers," PLOS Computational Biology, Public Library of Science, vol. 10(10), pages 1-11, October.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:479:y:2011:i:7374:d:10.1038_nature10545. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.