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Aggregation and vesiculation of membrane proteins by curvature-mediated interactions

Benedict J. Reynwar, Gregoria Illya, Vagelis A. Harmandaris, Martin M. Müller, Kurt Kremer () and Markus Deserno ()
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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

Nature, 2007, vol. 447, issue 7143, 461-464

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.

Date: 2007
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DOI: 10.1038/nature05840

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