EHD2 regulates caveolar dynamics via ATP-driven targeting and oligomerization
Moren, B. LU
; Shah, C.
; Howes, M. T.
; Schieber, N. L.
; Mcmahon, H. T.
; Parton, R. G.
; Daumke, O.
and Lundmark, R.
(2012)
In Molecular Biology of the Cell
23(7).
p.1316-1329
- Abstract
- Eps15 homology domain-containing 2 (EHD2) belongs to the EHD-containing protein family of dynamin-related ATPases involved in membrane remodeling in the endosomal system. EHD2 dimers oligomerize into rings on highly curved membranes, resulting in stimulation of the intrinsic ATPase activity. In this paper, we report that EHD2 is specifically and stably associated with caveolae at the plasma membrane and not involved in clathrin-mediated endocytosis or endosomal recycling, as previously suggested. EHD2 interacts with pacsin2 and cavin1, and ordered membrane assembly of EHD2 is dependent on cavin1 and caveolar integrity. While the EHD of EHD2 is dispensable for targeting, we identified a loop in the nucleotide-binding domain that, together... (More)
- Eps15 homology domain-containing 2 (EHD2) belongs to the EHD-containing protein family of dynamin-related ATPases involved in membrane remodeling in the endosomal system. EHD2 dimers oligomerize into rings on highly curved membranes, resulting in stimulation of the intrinsic ATPase activity. In this paper, we report that EHD2 is specifically and stably associated with caveolae at the plasma membrane and not involved in clathrin-mediated endocytosis or endosomal recycling, as previously suggested. EHD2 interacts with pacsin2 and cavin1, and ordered membrane assembly of EHD2 is dependent on cavin1 and caveolar integrity. While the EHD of EHD2 is dispensable for targeting, we identified a loop in the nucleotide-binding domain that, together with ATP binding, is required for caveolar localization. EHD2 was not essential for the formation or shaping of caveolae, but high levels of EHD2 caused distortion and loss of endogenous caveolae. Assembly of EHD2 stabilized and constrained caveolae to the plasma membrane to control turnover, and depletion of EHD2, resulting in endocytic and more dynamic and short-lived caveolae. Thus, following the identification of caveolin and cavins, EHD2 constitutes a third structural component of caveolae involved in controlling the stability and turnover of this organelle. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/d53723de-4b48-424f-8038-cc0633e96122
- author
- Moren, B.
LU
; Shah, C.
; Howes, M. T.
; Schieber, N. L.
; Mcmahon, H. T.
; Parton, R. G.
; Daumke, O.
and Lundmark, R.
- publishing date
- 2012-04-01
- type
- Contribution to journal
- publication status
- published
- in
- Molecular Biology of the Cell
- volume
- 23
- issue
- 7
- pages
- 1316 - 1329
- publisher
- American Society for Cell Biology
- external identifiers
-
- scopus:84859396266
- ISSN
- 1059-1524
- DOI
- 10.1091/mbc.E11-09-0787
- language
- English
- LU publication?
- no
- id
- d53723de-4b48-424f-8038-cc0633e96122
- alternative location
- http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E11-09-0787
- date added to LUP
- 2017-07-06 14:24:46
- date last changed
- 2022-01-30 21:26:56
@article{d53723de-4b48-424f-8038-cc0633e96122,
abstract = {{Eps15 homology domain-containing 2 (EHD2) belongs to the EHD-containing protein family of dynamin-related ATPases involved in membrane remodeling in the endosomal system. EHD2 dimers oligomerize into rings on highly curved membranes, resulting in stimulation of the intrinsic ATPase activity. In this paper, we report that EHD2 is specifically and stably associated with caveolae at the plasma membrane and not involved in clathrin-mediated endocytosis or endosomal recycling, as previously suggested. EHD2 interacts with pacsin2 and cavin1, and ordered membrane assembly of EHD2 is dependent on cavin1 and caveolar integrity. While the EHD of EHD2 is dispensable for targeting, we identified a loop in the nucleotide-binding domain that, together with ATP binding, is required for caveolar localization. EHD2 was not essential for the formation or shaping of caveolae, but high levels of EHD2 caused distortion and loss of endogenous caveolae. Assembly of EHD2 stabilized and constrained caveolae to the plasma membrane to control turnover, and depletion of EHD2, resulting in endocytic and more dynamic and short-lived caveolae. Thus, following the identification of caveolin and cavins, EHD2 constitutes a third structural component of caveolae involved in controlling the stability and turnover of this organelle.}},
author = {{Moren, B. and Shah, C. and Howes, M. T. and Schieber, N. L. and Mcmahon, H. T. and Parton, R. G. and Daumke, O. and Lundmark, R.}},
issn = {{1059-1524}},
language = {{eng}},
month = {{04}},
number = {{7}},
pages = {{1316--1329}},
publisher = {{American Society for Cell Biology}},
series = {{Molecular Biology of the Cell}},
title = {{EHD2 regulates caveolar dynamics via ATP-driven targeting and oligomerization}},
url = {{http://dx.doi.org/10.1091/mbc.E11-09-0787}},
doi = {{10.1091/mbc.E11-09-0787}},
volume = {{23}},
year = {{2012}},
}