en
Scientific article
Open access
English

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

Published inEMBO Journal, vol. 31, no. 10, p. 2350-2364
Publication date2012
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
Affiliation Not a UNIGE publication
Funding
  • Autre - 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
Main files (1)
Article (Published version)
Identifiers
ISSN of the journal0261-4189
234views
115downloads

Technical informations

Creation09/11/2019 1:32:00 PM
First validation09/11/2019 1:32:00 PM
Update time03/15/2023 6:00:21 PM
Status update03/15/2023 6:00:21 PM
Last indexation02/12/2024 1:04:27 PM
All rights reserved by Archive ouverte UNIGE and the University of GenevaunigeBlack