Evidence map›Paper›PMID 26030874›Full record

ArticleNature structural & molecular biology2015

Dynamic binding mode of a Synaptotagmin-1-SNARE complex in solution.

Kyle D Brewer, Taulant Bacaj, Andrea Cavalli, Carlo Camilloni, James D Swarbrick, Jin Liu, Amy Zhou, Peng Zhou, Nicholas Barlow, Junjie Xu and 10 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
–field-weighted citation impact
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

95 citing papers in PubMed.

  1. Review
  2. Review
  3. A lever hypothesis for Synaptotagmin-1 action in neurotransmitter release.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Neurotransmitter release is triggered by a calcium-induced rearrangement in the Synaptotagmin-1/SNARE complex primary interface.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Dynamic Formation of the Protein-Lipid Pre-fusion Complex.bioRxiv : the preprint server for biology · 2024
    Article
  10. Complexin has a dual synaptic function as checkpoint protein in vesicle priming and as a promoter of vesicle fusion.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Article
  13. Review
  14. The Core Complex of the CaJournal of molecular biology · 2023
    Review
  15. Calcium Sensors of Neurotransmitter Release.Advances in neurobiology · 2023
    Article
  16. SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023
    Article
  17. Article
  18. Article
  19. Review
  20. Article

35 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

20 authors.

Kyle D Brewer1] Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [2] Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [3] Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas, USA.
Taulant Bacaj1] Department of Molecular and Cellular Physiology, Stanford University Medical School, Stanford, California, USA. [2] Howard Hughes Medical Institute, Stanford University Medical School, Stanford, California, USA.
Andrea Cavalli1] Institute for Research in Biomedicine, Bellinzona, Switzerland. [2] Department of Chemistry, University of Cambridge, Cambridge, UK.
Carlo CamilloniDepartment of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000000299238590
James D SwarbrickMonash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria, Australia.
Jin Liu1] Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [2] Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [3] Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [4] Department of Chemistry, Southern Methodist University, Dallas, Texas, USA.
Amy Zhou1] Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [2] Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [3] Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas, USA.
Peng Zhou1] Department of Molecular and Cellular Physiology, Stanford University Medical School, Stanford, California, USA. [2] Howard Hughes Medical Institute, Stanford University Medical School, Stanford, California, USA.
Nicholas BarlowMonash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria, Australia.
Junjie Xu1] Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [2] Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [3] Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas, USA.
Alpay B Seven1] Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [2] Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [3] Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas, USA.
Eric A Prinslow1] Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [2] Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [3] Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas, USA.
Rashmi Voleti1] Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [2] Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [3] Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas, USA.
Daniel HäussingerDepartment of Chemistry, University of Basel, Basel, Switzerland.
Alexandre M J J BonvinBijvoet Center for Biomolecular Research, Faculty of Science, Utrecht University, Utrecht, the Netherlands.
Diana R Tomchick1] Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [2] Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas, USA.
Michele VendruscoloDepartment of Chemistry, University of Cambridge, Cambridge, UK.
Bim GrahamMonash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria, Australia.
Thomas C Südhof1] Department of Molecular and Cellular Physiology, Stanford University Medical School, Stanford, California, USA. [2] Howard Hughes Medical Institute, Stanford University Medical School, Stanford, California, USA.
Josep Rizo1] Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [2] Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas, USA. [3] Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas, USA.

Funding

SYNAPTOTAGMIN AND C2 DOMAINS--STRUCTURE AND FUNCTIONR01NS040944 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI RIZOREY, JOSE · 2001 to 2016
$6.4M
Molecular Biophysics Predoctoral Training ProgramT32GM008297 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI CHOOK, YUH MIN · 1989 to 2018
$2.4M
600MHz Varian VNMRS Console UpgradeS10RR026461 · NCRR · UT SOUTHWESTERN MEDICAL CENTER · PI ROSEN, MICHAEL K · 2010 to 2010
$254k
Postsynaptic Calcium Sensors in Synaptic PlasticityK99NS087086 · NINDS · STANFORD UNIVERSITY · PI BACAJ, TAULANT · 2014 to 2014
$75k
NCRR NIH HHS S10 RR026461NIGMS NIH HHS T32 GM008297NINDS NIH HHS K99 NS087086NINDS NIH HHS K99NS087086NINDS NIH HHS NS040944NINDS NIH HHS R01 NS040944
6 · The paper itself

Abstract

Rapid neurotransmitter release depends on the Ca2+ sensor Synaptotagmin-1 (Syt1) and the SNARE complex formed by synaptobrevin, syntaxin-1 and SNAP-25. How Syt1 triggers release has been unclear, partly because elucidating high-resolution structures of Syt1-SNARE complexes has been challenging. An NMR approach based on lanthanide-induced pseudocontact shifts now reveals a dynamic binding mode in which basic residues in the concave side of the Syt1 C2B-domain β-sandwich interact with a polyacidic region of the SNARE complex formed by syntaxin-1 and SNAP-25. The physiological relevance of this dynamic structural model is supported by mutations in basic residues of Syt1 that markedly impair SNARE-complex binding in vitro and Syt1 function in neurons. Mutations with milder effects on binding have correspondingly milder effects on Syt1 function. Our results support a model whereby dynamic interaction facilitates cooperation between Syt1 and the SNAREs in inducing membrane fusion.

Indexed as

AnimalsCells, CulturedHumansMice, Inbred C57BLModels, MolecularNeuronsNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Structure, TertiaryRatsSNARE ProteinsSynaptotagmin ISNARE ProteinsSynaptotagmin I

Identifiers

PMID26030874
PMCPMC4496268

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Registered trials

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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.