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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
Comptes Rendus Biologies
|July 31, 2003
Summary
Dynamin proteins, crucial for cell membrane processes, may self-assemble around lipid tubules. This mechanism could explain how dynamins form collars during vesicle scission, a key step in endocytosis.
Area of Science:
- Biophysics
- Cell Biology
- Molecular Dynamics
Background:
- Dynamin, a key protein in clathrin-mediated endocytosis, interacts with lipid bilayers.
- Structural studies reveal dynamin insertion into membranes and self-assembly around lipid tubules.
Purpose of the Study:
- To investigate the physical mechanism by which membrane-inserted dynamins contribute to vesicle scission.
- To hypothesize how dynamin's membrane curvature imprinting drives collective behavior.
Main Methods:
- Computational modeling of many-body interactions between dynamins and a membrane bud.
- Analysis of membrane elasticity and induced cylindrical curvature.
Main Results:
- Dynamins imprint local cylindrical curvature onto the membrane.
- Elastic forces recruit dynamins to membrane buds, forming a collar structure.
- This collar formation resembles the process preceding vesicle scission.
Conclusions:
- A biophysical model explains dynamin recruitment during endocytosis.
- Membrane-bound dynamin's curvature imprinting and elastic interactions are key to vesicle scission.
- This mechanism may underlie dynamin recruitment by clathrin coats.