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Caveolae are specialized domains present in the plasma membrane (PM) of mostmammalian cell types. They function in signalling, membrane regulation, andendocytosis. We found that the Eps‐15 homology domain‐containing protein 2 (EHD2, anATPase) associated with the static population of PM caveolae. Recruitment to the PMinvolved ATP binding, interaction with anionic lipids, and oligomerization intolarge complexes (60–75S) via interaction of the EH domains with intrinsicNPF/KPF motifs. Hydrolysis of ATP was essential for binding of EHD2 complexes tocaveolae. EHD2 was found to undergo dynamic exchange at caveolae, a process thatdepended on a functional ATPase cycle. Depletion of EHD2 by siRNA or expression of adominant‐negative mutant dramatically increased the fraction of mobile caveolarvesicles coming from the PM. Overexpression of EHD2, in turn, caused confinement ofcholera toxin B in caveolae. The confining role of EHD2 relied on its capacity tolink caveolae to actin filaments. Thus, EHD2 likely plays a key role in adjustingthe balance between PM functions of stationary caveolae and the role of caveolae asvesicular carriers.

Oligomers of the ATPase EHD2 confine caveolae to the plasma membrane through association with actin