Dynamin, unlike many GTPase superfamily members, exhibits a relatively rapid basal rate of GTP hydrolysis that is not rate-limited by GTP binding or GDP dissociation. Also unique to dynamin GTPase family members is their ability to self-assemble into rings and helical stacks of rings either in solution or onto lipid templates. Self-assembly stimulates dynamin's GTPase activity by >100-fold. Given these robust rates of GTP hydrolysis compared to most GTPases, GTP hydrolysis by dynamin can be easily measured using a simple colorimetic assay to detect released phosphate. We describe this assay and report variations in assay conditions that have contributed to the wide range of reported values for dynamin's basal and assembly-stimulated rates of GTP hydrolysis.
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