The GTPase dynamin is essential for CME (clathrin-mediated endocytosis), but its exact function and mechanism of action have been controversial. Here, we review findings that have led to the current models for dynamin function, either as a mechanochemical enzyme driving membrane fission or as a regulatory GTPase monitoring rate-limiting steps in CME. However, these models are not mutually exclusive and subsequent studies have provided evidence for both dynamin functions. Recent evidence derived from divergent in vivo and in vitro approaches suggests that dynamin plays a dual role in CME, functioning at early stages as a fidelity monitor to regulate clathrin-coated pit maturation and at later stages to directly catalyse membrane fission and clathrin-coated vesicle formation.

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