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Oligomers of the ATPase EHD2 confine caveolae to the plasma membrane through association with actin |
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Authors | ||
Published in | EMBO Journal. 2012, vol. 31, no. 10, p. 2350-2364 | |
Abstract | Caveolae are specialized domains present in the plasma membrane (PM) of most mammalian cell types. They function in signalling, membrane regulation, and endocytosis. We found that the Eps-15 homology domain-containing protein 2 (EHD2, an ATPase) associated with the static population of PM caveolae. Recruitment to the PM involved ATP binding, interaction with anionic lipids, and oligomerization into large complexes (60-75S) via interaction of the EH domains with intrinsic NPF/KPF motifs. Hydrolysis of ATP was essential for binding of EHD2 complexes to caveolae. EHD2 was found to undergo dynamic exchange at caveolae, a process that depended on a functional ATPase cycle. Depletion of EHD2 by siRNA or expression of a dominant-negative mutant dramatically increased the fraction of mobile caveolar vesicles coming from the PM. Overexpression of EHD2, in turn, caused confinement of cholera toxin B in caveolae. The confining role of EHD2 relied on its capacity to link caveolae to actin filaments. Thus, EHD2 likely plays a key role in adjusting the balance between PM functions of stationary caveolae and the role of caveolae as vesicular carriers. | |
Keywords | Actins/metabolism — Adenosine Triphosphate/metabolism — Carrier Proteins/genetics/metabolism — Caveolae/metabolism — Cell Membrane/metabolism — Gene Deletion — Gene Expression — Gene Silencing — HeLa Cells — Humans — Protein Binding — Protein Interaction Domains and Motifs | |
Identifiers | PMID: 22505029 | |
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Research group | Contrôle subcellulaire des récepteurs de signalisation (1005) | |
Project | Boehringer Ingelheim Fonds PhD fellowship | |
Citation (ISO format) | STOEBER, Miriam Carolin et al. Oligomers of the ATPase EHD2 confine caveolae to the plasma membrane through association with actin. In: EMBO Journal, 2012, vol. 31, n° 10, p. 2350-2364. doi: 10.1038/emboj.2012.98 https://archive-ouverte.unige.ch/unige:123107 |