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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

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Volume 395, Issue 3

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Reshaping biological membranes in endocytosis: crossing the configurational space of membrane-protein interactions

Mijo Simunovic
  • Institut Curie, Centre National de la Recherche Scientifique Unité Mixte de Recherche 168, Université Pierre et Marie Curie, F-75248 Paris, France
  • Department of Physics, Université Paris Diderot, 10, rue Alice Domon et Léonie Duquet, 75013 Paris, France
  • Department of Chemistry, The University of Chicago, Chicago, IL 60637, USA
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Patricia Bassereau
  • Corresponding author
  • Institut Curie, Centre National de la Recherche Scientifique Unité Mixte de Recherche 168, Université Pierre et Marie Curie, F-75248 Paris, France
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2013-12-17 | DOI: https://doi.org/10.1515/hsz-2013-0242

Abstract

Lipid membranes are highly dynamic. Over several decades, physicists and biologists have uncovered a number of ways they can change the shape of membranes or alter their phase behavior. In cells, the intricate action of membrane proteins drives these processes. Considering the highly complex ways proteins interact with biological membranes, molecular mechanisms of membrane remodeling still remain unclear. When studying membrane remodeling phenomena, researchers often observe different results, leading them to disparate conclusions on the physiological course of such processes. Here we discuss how combining research methodologies and various experimental conditions contributes to the understanding of the entire phase space of membrane-protein interactions. Using the example of clathrin-mediated endocytosis we try to distinguish the question ‘how can proteins remodel the membrane?’ from ‘how do proteins remodel the membrane in the cell?’ In particular, we consider how altering physical parameters may affect the way membrane is remodeled. Uncovering the full range of physical conditions under which membrane phenomena take place is key in understanding the way cells take advantage of membrane properties in carrying out their vital tasks.

Keywords: BAR domain; clathrin; membrane remodeling; membrane tension; multiscale simulation

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About the article

Mijo Simunovic

Mijo Simunovic is a PhD student in chemistry at the University of Chicago and in physics at the Curie Institute in Paris. In his research, he combines coarse-grained theoretical techniques in the Voth group with experimental biophysical methods at the Bassereau group to study the physics underlying protein-induced membrane remodeling phenomena. Before joining these two groups, he received his BS and MS in physical chemistry from the University of Zagreb, where he employed theoretical and experimental approaches in investigating problems in synthetic and quantum chemistry.

Patricia Bassereau

Patricia Bassereau is currently Directrice de Recherche, CNRS at the Curie Institute in Paris. After spending 7 years in Montpellier (GDPC) working on the structure of surfactant-based phases, and a year as a visiting scientist at the Almaden IBM Center (San Jose, USA) on the structure of thin polymer films, she moved in 1993 to the Curie Institute. She initially investigated the interactions of soluble proteins with polymer monolayers. In the last 15 years, she has been working in the field of ‘physics for cell biology’. She has developed a multidisciplinary approach to understand the role of lipid membranes in important cellular functions such as intracellular trafficking, endo/exocytosis, transmembrane ion transport (‘active membranes’), or cell adhesion.


Corresponding author: Patricia Bassereau, Institut Curie, Centre National de la Recherche Scientifique Unité Mixte de Recherche 168, Université Pierre et Marie Curie, F-75248 Paris, France, e-mail:


Received: 2013-08-20

Accepted: 2013-12-16

Published Online: 2013-12-17

Published in Print: 2014-03-01


Citation Information: Biological Chemistry, Volume 395, Issue 3, Pages 275–283, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2013-0242.

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