Evidence map›Paper›PMID 24782308›Full record

ArticleThe Journal of biological chemistry2014

Differential interaction of tomosyn with syntaxin and SNAP25 depends on domains in the WD40 β-propeller core and determines its inhibitory activity.

Noa Bielopolski, Alice D Lam, Dana Bar-On, Markus Sauer, Edward L Stuenkel, Uri Ashery

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

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  12. Dynamic Partitioning of Synaptic Vesicle Pools by the SNARE-Binding Protein Tomosyn.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    Article
  13. Article
  14. Review
  15. Article
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  17. Review
  18. Quantitative analysis of single-molecule superresolution images.Current opinion in structural biology · 2014
    Review
  19. 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

6 authors at 3 institutions in 3 countries.

Noa BielopolskiFrom the Department of Neurobiology, Life Sciences Faculty, and.
Alice D Lamthe Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, Michigan 48109, and.
Dana Bar-OnFrom the Department of Neurobiology, Life Sciences Faculty, and Sagol School of Neuroscience, Tel Aviv University, 69978 Tel Aviv, Israel.
Markus Sauerthe Department of Biotechnology and Biophysics, Julius Maximilians University Würzburg, Am Hubland, 97074 Würzburg, Germany.
Edward L Stuenkelthe Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, Michigan 48109, and.
Uri AsheryFrom the Department of Neurobiology, Life Sciences Faculty, and Sagol School of Neuroscience, Tel Aviv University, 69978 Tel Aviv, Israel, uria@post.tau.ac.il.
Tel Aviv University · ILUniversity of Michigan–Ann Arbor · USUniversity of Würzburg · DE

Funding

Regulation of tomosyn-SNARE complex assembly in neurosecretionR01NS053978 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI STUENKEL, EDWARD L · 2006 to 2010
$1.6M
NINDS NIH HHS R01 NS053978
6 · The paper itself

Abstract

Neuronal exocytosis depends on efficient formation of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes and is regulated by tomosyn, a SNARE-binding protein. To gain new information about tomosyn's activity, we characterized its mobility and organization on the plasma membrane (PM) in relation to other SNARE proteins and inhibition of exocytosis. By using direct stochastic optical reconstruction microscopy (dSTORM), we found tomosyn to be organized in small clusters adjacent to syntaxin clusters. In addition, we show that tomosyn is present in both syntaxin-tomosyn complexes and syntaxin-SNAP25-tomosyn complexes. Tomosyn mutants that lack residues 537-578 or 897-917 from its β-propeller core diffused faster on the PM and exhibited reduced binding to SNAP25, suggesting that these mutants shift the equilibrium between tomosyn-syntaxin-SNAP25 complexes on the PM to tomosyn-syntaxin complexes. As these deletion mutants impose less inhibition on exocytosis, we suggest that tomosyn inhibition is mediated via tomosyn-syntaxin-SNAP25 complexes and not tomosyn-syntaxin complexes. These findings characterize, for the first time, tomosyn's dynamics at the PM and its relation to its inhibition of exocytosis.

Indexed as

AnimalsBinding SitesCell MembraneExocytosisGene DeletionHEK293 CellsHumansMiceNerve Tissue ProteinsPC12 CellsProtein BindingProtein TransportRatsR-SNARE ProteinsSynaptosomal-Associated Protein 25Syntaxin 1Nerve Tissue ProteinsR-SNARE ProteinsSnap25 protein, ratStx1a protein, ratStxbp5 protein, ratSynaptosomal-Associated Protein 25Syntaxin 1ExocytosisFRAPMembrane FusionMicroscopyNeurobiologySNARE ProteinsTomosyn

Identifiers

PMID24782308
PMCPMC4059150
OpenAlexW2018033288

What OpenQuestion holds

Textmetadata
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.