English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  v-SNARE transmembrane domains function as catalysts for vesicle fusion.

Dhara, M., Yarzagaray, A., Makke, M., Schindeldecker, B., Schwarz, Y., Shaaban, A., et al. (2016). v-SNARE transmembrane domains function as catalysts for vesicle fusion. eLife, 5: e17571. doi:10.7554/eLife.17571.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-4316-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-4319-5
Genre: Journal Article

Files

show Files
hide Files
:
2339866.pdf (Publisher version), 7MB
Name:
2339866.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-

Locators

show

Creators

show
hide
 Creators:
Dhara, M., Author
Yarzagaray, A., Author
Makke, M., Author
Schindeldecker, B., Author
Schwarz, Y., Author
Shaaban, A., Author
Sharma, S.1, Author              
Böckmann, R.A, Author
Lindau, M.1, Author              
Mohrmann, R., Author
Bruns, D., Author
Affiliations:
1Research Group of Nanoscale Cell Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1832294              

Content

show
hide
Free keywords: exocytosis; membrane fusion; mouse; neuroscience; neurotransmitter release; synaptobrevin
 Abstract: Vesicle fusion is mediated by an assembly of SNARE proteins between opposing membranes, but it is unknown whether transmembrane domains (TMDs) of SNARE proteins serve mechanistic functions that go beyond passive anchoring of the force-generating SNAREpin to the fusing membranes. Here, we show that conformational flexibility of synaptobrevin-2 TMD is essential for efficient Ca(2+)-triggered exocytosis and actively promotes membrane fusion as well as fusion pore expansion. Specifically, the introduction of helix-stabilizing leucine residues within the TMD region spanning the vesicle's outer leaflet strongly impairs exocytosis and decelerates fusion pore dilation. In contrast, increasing the number of helix-destabilizing, ß-branched valine or isoleucine residues within the TMD restores normal secretion but accelerates fusion pore expansion beyond the rate found for the wildtype protein. These observations provide evidence that the synaptobrevin-2 TMD catalyzes the fusion process by its structural flexibility, actively setting the pace of fusion pore expansion.

Details

show
hide
Language(s): eng - English
 Dates: 2016-06-25
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.7554/eLife.17571
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: eLife
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: 25 Volume / Issue: 5 Sequence Number: e17571 Start / End Page: - Identifier: -