English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2

Shah, C., Hegde, B. G., Morén, B., Behrmann, E., Mielke, T., Moenke, G., et al. (2014). Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2. Structure, 22(3), 409-420. doi:10.1016/j.str.2013.12.015.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0000-70A6-6 Version Permalink: http://hdl.handle.net/21.11116/0000-0000-70A8-4
Genre: Journal Article

Files

show Files
hide Files
:
Shah.pdf (Publisher version), 4MB
Name:
Shah.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
© 2014 Elsevier Ltd
License:
-

Locators

show

Creators

show
hide
 Creators:
Shah, C., Author
Hegde, B. G., Author
Morén, B., Author
Behrmann, E., Author
Mielke, T.1, Author              
Moenke, G., Author
Spahn, C. M. T., Author
Lundmark, R., Author
Daumke, O., Author
Langen, R., Author
Affiliations:
1Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              

Content

show
hide
Free keywords: -
 Abstract: The dynamin-related Eps15-homology domain-containing protein 2 (EHD2) is a membrane-remodeling ATPase that regulates the dynamics of caveolae. Here, we established an electron paramagnetic resonance (EPR) approach to characterize structural features of membrane-bound EHD2. We show that residues at the tip of the helical domain can insert into the membrane and may create membrane curvature by a wedging mechanism. Using EPR and X-ray crystallography, we found that the N terminus is folded into a hydrophobic pocket of the GTPase domain in solution and can be released into the membrane. Cryoelectron microscopy demonstrated that the N terminus is not essential for oligomerization of EHD2 into a membrane-anchored scaffold. Instead, we found a function of the N terminus in regulating targeting and stable association of EHD2 to caveolae. Our data uncover an unexpected, membrane-induced regulatory switch in EHD2 and demonstrate the versatility of EPR to study structure and function of dynamin superfamily proteins.

Details

show
hide
Language(s): eng - English
 Dates: 2014-03-04
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1016/j.str.2013.12.015
ISSN: 1878-4186 (Electronic)
ISSN: 0969-2126 (Print)
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Structure
  Other : Structure
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Cell Press
Pages: - Volume / Issue: 22 (3) Sequence Number: - Start / End Page: 409 - 420 Identifier: ISSN: 0969-2126
CoNE: /journals/resource/954927002244_1