%0 Book Section %1 statphys23_1086 %A Lenz, M. %A Joanny, J.F. %A Prost, J. %B Abstract Book of the XXIII IUPAP International Conference on Statistical Physics %C Genova, Italy %D 2007 %E Pietronero, Luciano %E Loreto, Vittorio %E Zapperi, Stefano %K dynamin interaction molecular motors protein-membrane statphys23 topic-10 %T Dynamin as a molecular motor: a thermodynamic study %U http://st23.statphys23.org/webservices/abstract/preview_pop.php?ID_PAPER=1086 %X Dynamin is a GTPase implicated in the severing of cell membrane during endocytosis. Recent in vitro experiments have shown that it is a molecular motor: when polymerized in a helical shape around a membrane nanotube, it can drag a polystyrene bead along with its rotation and form supercoils. We model the dynamin-membrane assembly in order to extract information from this and future experimental data about the mechanical mode of action of dynamin, a topic still under debate. Our first results concern the long dynamin/membrane tubes used in in vitro experiments: their dynamics is dominated by the relaxation of the membrane and dynamin helix deformations through helix-membrane friction. Little is known about this mechanism on the molecular level, but our coarse-grained out-of-equilibrium thermodynamical approach allows us to characterize it. This model and data from ongoing experiments in Institut Curie should allow us to know more about the role of dynamin in endocytosis.

@incollection{statphys23_1086, abstract = {Dynamin is a GTPase implicated in the severing of cell membrane during endocytosis. Recent in vitro experiments have shown that it is a molecular motor: when polymerized in a helical shape around a membrane nanotube, it can drag a polystyrene bead along with its rotation and form supercoils. We model the dynamin-membrane assembly in order to extract information from this and future experimental data about the mechanical mode of action of dynamin, a topic still under debate. Our first results concern the long dynamin/membrane tubes used in in vitro experiments: their dynamics is dominated by the relaxation of the membrane and dynamin helix deformations through helix-membrane friction. Little is known about this mechanism on the molecular level, but our coarse-grained out-of-equilibrium thermodynamical approach allows us to characterize it. This model and data from ongoing experiments in Institut Curie should allow us to know more about the role of dynamin in endocytosis.}, added-at = {2007-06-20T10:16:09.000+0200}, address = {Genova, Italy}, author = {Lenz, M. and Joanny, J.F. and Prost, J.}, biburl = {https://www.bibsonomy.org/bibtex/2923a24d50839e1869fc99f92073b5eb2/statphys23}, booktitle = {Abstract Book of the XXIII IUPAP International Conference on Statistical Physics}, editor = {Pietronero, Luciano and Loreto, Vittorio and Zapperi, Stefano}, interhash = {5c46409594a307dd828e4bc3e884ec1f}, intrahash = {923a24d50839e1869fc99f92073b5eb2}, keywords = {dynamin interaction molecular motors protein-membrane statphys23 topic-10}, month = {9-13 July}, timestamp = {2007-06-20T10:16:38.000+0200}, title = {Dynamin as a molecular motor: a thermodynamic study}, url = {http://st23.statphys23.org/webservices/abstract/preview_pop.php?ID_PAPER=1086}, year = 2007 }