Evidence map›Paper›PMID 20688915›Full record

ArticleThe Journal of biological chemistry2010

Rat and Drosophila synaptotagmin 4 have opposite effects during SNARE-catalyzed membrane fusion.

Zhao Wang, Edwin R Chapman

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Synaptotagmin-1 is a CaCell reports · 2023
    Article
  7. Article
  8. Function of Drosophila Synaptotagmins in membrane trafficking at synapses.Cellular and molecular life sciences : CMLS · 2021
    Review
  9. Transcriptional Correlates of Chronic Alcohol Neuroadaptation inFrontiers in behavioral neuroscience · 2021
    Article
  10. Article
  11. Article
  12. Gliocrine System: Astroglia as Secretory Cells of the CNS.Advances in experimental medicine and biology · 2019
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Distinct subsets of Syt-IV/BDNF vesicles are sorted to axons versus dendrites and recruited to synapses by activity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
  20. Review
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

2 authors at 1 institution in 1 country.

Zhao WangDepartment of Physiology, Howard Hughes Medical Institute, University of Wisconsin, Madison, Wisconsin 53706, USA.
Edwin R Chapman
Howard Hughes Medical Institute · US

Funding

Synaptotagmin C2B Domain as a Ca2+ Sensing ModuleR01MH061876 · NIMH · UNIVERSITY OF WISCONSIN-MADISON · PI Edwin R Chapman · 2002 to 2026
$7.7M
Howard Hughes Medical InstituteNIMH NIH HHS MH 61876NIMH NIH HHS R01 MH061876
6 · The paper itself

Abstract

Synaptotagmins (Syt) are a large family of proteins that regulate membrane traffic in neurons and other cell types. One isoform that has received considerable attention is SYT4, with apparently contradictory reports concerning the function of this isoform in fruit flies and mice. SYT4 was reported to function as a negative regulator of neurotrophin secretion in mouse neurons and as a positive regulator of secretion of a yet to be identified growth factor from muscle cells in flies. Here, we have directly compared the biochemical and functional properties of rat and fly SYT4. We report that rat SYT4 inhibited SNARE-catalyzed membrane fusion in both the absence and presence of Ca(2+). In marked contrast, fly SYT4 stimulated SNARE-mediated membrane fusion in response to Ca(2+). Analysis of chimeric molecules, isolated C2 domains, and point mutants revealed that the C2B domain of the fly protein senses Ca(2+) and is sufficient to stimulate fusion. Rat SYT4 was able to stimulate fusion in response to Ca(2+) when the conserved Asp-to-Ser Ca(2+) ligand substitution in its C2A domain was reversed. In summary, rat SYT4 serves as an inhibitory isoform, whereas fly SYT4 is a bona fide Ca(2+) sensor capable of coupling Ca(2+) to membrane fusion.

Indexed as

AnimalsCalciumDrosophila melanogasterMembrane FusionMicePoint MutationProtein Structure, TertiaryRatsRecombinant Fusion ProteinsSNARE ProteinsSpecies SpecificitySynaptotagminsCalciumRecombinant Fusion ProteinsSNARE ProteinsSynaptotagminsSyt4 protein, rat

Identifiers

PMID20688915
PMCPMC2945570
OpenAlexW2086025021

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.