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Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
Published on: October 20, 2014
Dynamin recruitment by clathrin coats: a physical step?
Jean-Baptiste Fournier1, Paul G Dommersnes, Paola Galatola
1Laboratoire de physico-chimie théorique, FR CNRS 2438 Matière et Systèmes complexes, ESPCI, 10, rue Vauquelin, 75231 Paris, France. jbf@turner.pct.espci.fr
Abstract:
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.
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