GTPase activity of dynamin and resulting conformation change are essential for endocytosis

Bruno Marks, Michael H. B. Stowell, Yvonne Vallis, Ian G. Mills, Adele Gibson, Colin R. Hopkins and Harvey T. McMahon ()
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Bruno Marks: MRC Laboratory of Molecular Biology
Michael H. B. Stowell: MRC Laboratory of Molecular Biology
Yvonne Vallis: MRC Laboratory of Molecular Biology
Ian G. Mills: MRC Laboratory of Molecular Biology
Adele Gibson: MRC Laboratory for Molecular Cell Biology, University College London
Colin R. Hopkins: MRC Laboratory for Molecular Cell Biology, University College London
Harvey T. McMahon: MRC Laboratory of Molecular Biology

Nature, 2001, vol. 410, issue 6825, 231-235

Abstract: Abstract 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 processes1,2. 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 unclear3,4. It has been proposed that dynamin is a regulator (similar to classical G proteins) of downstream effectors5. 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.

Date: 2001
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DOI: 10.1038/35065645

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