| First Author | Stoeber M | Year | 2012 |
| Journal | EMBO J | Volume | 31 |
| Issue | 10 | Pages | 2350-64 |
| PubMed ID | 22505029 | Mgi Jnum | J:184695 |
| Mgi Id | MGI:5426089 | Doi | 10.1038/emboj.2012.98 |
| Citation | Stoeber M, et al. (2012) Oligomers of the ATPase EHD2 confine caveolae to the plasma membrane through association with actin. EMBO J 31(10):2350-64 |
| abstractText | 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. |
