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Aggregation and vesiculation of membrane proteins by curvature-mediated interactions

Author

Listed:
  • Benedict J. Reynwar

    (Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany)

  • Gregoria Illya

    (Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany)

  • Vagelis A. Harmandaris

    (Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany)

  • Martin M. Müller

    (Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany)

  • Kurt Kremer

    (Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany)

  • Markus Deserno

    (Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany)

Abstract

Follow the curve Cell membranes are far more than mere outer envelopes: remodelling of their topology is linked to vital tasks such as endocytosis, vesicle formation and protein sorting. Specialized proteins can sense and create membrane curvature, and direct membrane remodelling. Several proteins need to act together to accomplish this task, so a more generic, universal effect is thought to be at work as well. For years physicists, mathematicians, materials scientists and cell biologists have studied a possible universal effect — attraction between proteins that is induced solely by membrane curvature. But the nature of membrane-curvature-induced interactions between proteins, and even the question of whether they are attractive or repulsive, remained obscure. Now computer simulations reveal that curvature-induced interactions can indeed be attractive, strong, and robust. Well up to the task of effecting membrane remodelling. On the cover, a virtual membrane covered with capsids during cooperative budding.

Suggested Citation

  • Benedict J. Reynwar & Gregoria Illya & Vagelis A. Harmandaris & Martin M. Müller & Kurt Kremer & Markus Deserno, 2007. "Aggregation and vesiculation of membrane proteins by curvature-mediated interactions," Nature, Nature, vol. 447(7143), pages 461-464, May.
    • Handle: RePEc:nat:nature:v:447:y:2007:i:7143:d:10.1038_nature05840
    DOI: 10.1038/nature05840
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    Cited by:

    1. Yining Jiang & Batiste Thienpont & Vinay Sapuru & Richard K. Hite & Jeremy S. Dittman & James N. Sturgis & Simon Scheuring, 2022. "Membrane-mediated protein interactions drive membrane protein organization," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. Raluca Groza & Kita Valerie Schmidt & Paul Markus Müller & Paolo Ronchi & Claire Schlack-Leigers & Ursula Neu & Dmytro Puchkov & Rumiana Dimova & Claudia Matthaeus & Justin Taraska & Thomas R. Weikl &, 2024. "Adhesion energy controls lipid binding-mediated endocytosis," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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