English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Control of membrane gaps by ​synaptotagmin-Ca2+ measured with a novel membrane distance ruler.

Lin, C. C., Seikowski, J., Perez-Lara, A., Jahn, R., Höbartner, C., & Walla, P. J. (2014). Control of membrane gaps by ​synaptotagmin-Ca2+ measured with a novel membrane distance ruler. Nature Communications, 5: 5859. doi:10.1038/ncomms6859.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-B645-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-6EBC-0
Genre: Journal Article

Files

show Files
hide Files
:
2087480.pdf (Publisher version), 649KB
Name:
2087480.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
:
2087480_Suppl.pdf (Supplementary material), 412KB
Name:
2087480_Suppl.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Lin, C. C.1, Author              
Seikowski, J.2, Author              
Perez-Lara, A.3, Author              
Jahn, R.3, Author              
Höbartner, C.2, Author              
Walla, P. J.1, Author              
Affiliations:
1Research Group of Biomolecular Spectroscopy and Single-Molecule Detection, MPI for biophysical chemistry, Max Planck Society, ou_578565              
2Research Group of Nucleic Acid Chemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578605              
3Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              

Content

show
hide
Free keywords: -
 Abstract: Fast synchronous neurotransmitter release is triggered by calcium that activates ​synaptotagmin-1 (​syt-1), resulting in fusion of synaptic vesicles with the presynaptic membrane. ​Syt-1 possesses two Ca2+-binding C2 domains that tether membranes via interactions with anionic phospholipids. It is capable of crosslinking membranes and has recently been speculated to trigger fusion by decreasing the gap between them. As quantitative information on membrane gaps is key to understanding general cellular mechanisms, including the role of ​syt-1, we developed a fluorescence-lifetime based inter-membrane distance ruler using membrane-anchored DNAs of various lengths as calibration standards. Wild-type and mutant data provide evidence that full-length ​syt-1 indeed regulates membrane gaps: without Ca2+, ​syt-1 maintains membranes at distances of ~7–8 nm. Activation with 100 μM Ca2+ decreases the distance to ~5 nm by binding the C2 domains to opposing membranes, respectively. These values reveal that activated ​syt-1 adjusts membrane distances to the level that promotes SNARE complex assembly.

Details

show
hide
Language(s): eng - English
 Dates: 2014-12-15
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/ncomms6859
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature Communications
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: 7 Volume / Issue: 5 Sequence Number: 5859 Start / End Page: - Identifier: -