Dynamin recruitment by clathrin coats: a physical step?
Recent structural findings have shown that dynamin, a cytosol protein playing a key-role in clathrin-mediated endocytosis, inserts partly within the lipid bilayer and tends to self-assemble around lipid tubules. Taking into account these observations, we make the hypothesis that individual membrane-inserted dynamins imprint a local cylindrical curvature to the membrane. This imprint may give rise to long-range mechanical forces mediated by the elasticity of the membrane. Calculating the resulting many-body interaction between a collection of inserted dynamins and a membrane bud, we find a regime in which the dynamins are elastically recruited by the bud to form a collar around its neck, which is reminiscent of the actual process preempting vesicle scission. This physical mechanism might therefore be implied in the recruitment of dynamins by clathrin coats.
Fournier
Jean-Baptiste
JB
Laboratoire de physico-chimie théorique, FR CNRS 2438 Matière et Systèmes complexes, ESPCI, 10, rue Vauquelin, 75231 Paris, France. jbf@turner.pct.espci.fr
Dommersnes
Paul G
PG
Galatola
Paola
P
D001696:Biomechanical Phenomena; D002462:Cell Membrane / Q000737:chemistry / Q000502:physiology* / Q000648:ultrastructure; D022163:Clathrin-Coated Vesicles / Q000378:metabolism*; D034281:Dynamins / Q000378:metabolism*; D004548:Elasticity; D008051:Lipid Bilayers / Q000378:metabolism; D008433:Mathematics; D008954:Models, Biological; D009010:Monte Carlo Method
D008051:Lipid Bilayers; D034281:Dynamins