Deformation of dynamin helices damped by membrane friction.
Dynamin and other proteins of the dynamin superfamily are widely used by cells to sever lipid bilayers. During this process, a short helical dynamin polymer (one to three helical turns) assembles around a membrane tubule and reduces its radius and pitch upon guanosine triphosphate hydrolysis. This deformation is thought to be crucial for dynamin's severing action and results in an observable twisting of the helix. Here, we quantitatively characterize the dynamics of this deformation by studying long dynamin helices (many helical turns). We perform in vitro experiments where we attach small beads to the dynamin helix and track their rotation in real time, thus collecting information about the space and time dependence of the deformation. We develop a theoretical formalism to predict the dynamics of a mechanically continuous helix deforming on long timescales. Longer helices deform more slowly, as predicted by theory. This could account for the previously reported observation that they are less fission-competent. Comparison between experiments and our model indicates that the deformation dynamics is dominated by the draining of the membrane out of the helix, allowing quantification of helix-membrane interactions.
Laboratoire Physico-Chimie Curie, Institut Curie, Centre de Recherche, Paris, France.
Sandrine
S
Morlot
Martin
M
Lenz
Jacques
J
Prost
Jean-François
JF
Joanny
Aurélien
A
Roux
D000818:Animals; D001696:Biomechanical Phenomena; D034281:Dynamins / Q000737:chemistry*; D017276:Friction; D006160:Guanosine Triphosphate / Q000378:metabolism; D057446:Hydrodynamics; D006868:Hydrolysis; D008567:Membranes, Artificial; D008863:Microspheres; D008970:Molecular Weight; D017433:Protein Structure, Secondary; D051381:Rats; D015203:Reproducibility of Results; D012399:Rotation; D013997:Time Factors
D008567:Membranes, Artificial; D006160:Guanosine Triphosphate; D034281:Dynamins