Evidence map›Paper›PMID 18508081›Full record

ArticleJournal of molecular biology2008

Cross-linking of phospholipid membranes is a conserved property of calcium-sensitive synaptotagmins.

Emma Connell, Asiya Giniatullina, Joséphine Lai-Kee-Him, Richard Tavare, Enrico Ferrari, Alan Roseman, Dan Cojoc, Alain R Brisson, Bazbek Davletov

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Doc2b CaScientific reports · 2019
    Article
  3. Review
  4. Article
  5. Prevalent mechanism of membrane bridging by synaptotagmin-1.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  6. Article
  7. Article
  8. Article
  9. Forming giant vesicles with controlled membrane composition, asymmetry, and contents.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  10. Article
  11. Synaptic vesicles studied by dynamic light scattering.The European physical journal. E, Soft matter · 2011
    Article
  12. Article
  13. Article
  14. Article
  15. Minimal membrane docking requirements revealed by reconstitution of Rab GTPase-dependent membrane fusion from purified components.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Emma ConnellMRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.
Asiya Giniatullina
Joséphine Lai-Kee-Him
Richard Tavare
Enrico Ferrari
Alan Roseman
Dan Cojoc
Alain R Brisson
Bazbek Davletov
MRC Laboratory of Molecular Biology · GBInstitut Européen de Chimie et Biologie · FRUniversité de Bordeaux · FR

Funding

Medical Research Council MC_U105178791
6 · The paper itself

Abstract

Synaptotagmins are vesicular proteins implicated in many membrane trafficking events. They are highly conserved in evolution and the mammalian family contains 16 isoforms. We now show that the tandem C2 domains of several calcium-sensitive synaptotagmin isoforms tested, including Drosophila synaptotagmin, rapidly cross-link phospholipid membranes. In contrast to the tandem structure, individual C2 domains failed to trigger membrane cross-linking in several novel assays. Large-scale liposomal aggregation driven by tandem C2 domains in response to calcium was confirmed by the following techniques: turbidity assay, dynamic light-scattering and both confocal and negative stain electron microscopy. Firm cross-linking of membranes was evident from laser trap experiments. High-resolution cryo-electron microscopy revealed that membrane cross-linking by tandem C2 domains results in a constant distance of approximately 9 nm between the apposed membranes. Our findings show the conserved nature of this important property of synaptotagmin, demonstrate the significance of the tandem C2 domain structure and provide a plausible explanation for the accelerating effect of synaptotagmins on membrane fusion.

Indexed as

AnimalsCalciumCross-Linking ReagentsCryoelectron MicroscopyDrosophila melanogasterPhospholipidsProtein Structure, TertiarySynaptotagminsUnilamellar LiposomesCalciumCross-Linking ReagentsPhospholipidsSynaptotagminsUnilamellar Liposomes

Identifiers

PMID18508081
PMCPMC2726287
OpenAlexW2008389970

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.