Abstract
In the final stage of endocytosis, the protein dynamin forms a helical protein coat around the vesicle neck that ultimately disrupts the lipid membrane and cuts the neck. Dynamin causes membrane scission by undergoing a large conformational change after catalyzing the hydrolysis of guanosine triphosphate (GTP) to guanosine diphosphate (GDP). Understanding how these allosteric changes are propagated through the dynamin oligomeric helix could help determine which protein-protein interaction are important for membrane scission. To this end, we have used molecular dynamics of dynamin dimers and tetramers in solution to understand the interplay between the dynamin protein contacts and the allosteric motions of the protein. By correlating the motions of the protein with observed protein contacts, we are able to understand which dynamin protein interactions may be key mediators of membrane fission.
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