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Dynamin is a large GTPase with a relative molecular mass of 96,000 (Mr 96K) that is involved in clathrin-mediated endocytosis and other vesicular trafficking processes. Although its function is apparently essential for scission of newly formed vesicles from the plasma membrane, the nature of dynamin's role in the scission process is still unclear. It has been proposed that dynamin is a regulator (similar to classical G proteins) of downstream effectors. Here we report the analysis of several point mutants of dynamin's GTPase effector (GED) and GTPase domains. We show that oligomerization and GTP binding alone, by dynamin, are not sufficient for endocytosis in vivo. Rather, efficient GTP hydrolysis and an associated conformational change are also required. These data argue that dynamin has a mechanochemical function in vesicle scission.

Original publication

DOI

10.1038/35065645

Type

Journal article

Journal

Nature

Publication Date

08/03/2001

Volume

410

Pages

231 - 235

Keywords

Amino Acid Sequence, Animals, COS Cells, Cattle, Drosophila, Dynamins, Endocytosis, GTP Phosphohydrolases, Guanosine Triphosphate, Humans, Hydrolysis, Molecular Sequence Data, Point Mutation, Protein Conformation, Protein Structure, Tertiary, Recombinant Fusion Proteins, Transferrin