Evidence map›Paper›PMID 24001110›Full record

ArticleThe Biochemical journal2013

The synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening.

Ying Lai, Xiaochu Lou, Yongseok Jho, Tae-Young Yoon, Yeon-Kyun Shin

Abstract read
In one paragraph

Article in The Biochemical journal, 2013. 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
–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

19 citing papers in PubMed.

  1. Membrane Merger Dynamics in Exocytosis and Endocytosis.Advances in experimental medicine and biology · 2026
    Review
  2. Review
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  7. Review
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  10. Phosphorylation of synaptotagmin-1 controls a post-priming step in PKC-dependent presynaptic plasticity.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. Article
  12. Article
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  14. Transmembrane tethering of synaptotagmin to synaptic vesicles controls multiple modes of neurotransmitter release.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  15. Article
  16. Article
  17. Article
  18. Article
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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

5 authors.

Ying Lai*Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, U.S.A.
Xiaochu Lou
Yongseok Jho
Tae-Young Yoon
Yeon-Kyun Shin

Funding

Regulations of SNARE-dependent membrane fusionR01GM051290 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI SHIN, YEON-KYUN · 1999 to 2019
$5.0M
NIGMS NIH HHS R01 GM051290
6 · The paper itself

Abstract

Syt1 (synaptotagmin 1), a major Ca2+ sensor for fast neurotransmitter release, contains tandem Ca2+-binding C2 domains (C2AB), a single transmembrane α-helix and a highly charged 60-residue-long linker in between. Using single-vesicle-docking and content-mixing assays we found that the linker region of Syt1 is essential for its two signature functions: Ca2+-independent vesicle docking and Ca2+-dependent fusion pore opening. The linker contains the basic-amino-acid-rich N-terminal region and the acidic-amino-acid-rich C-terminal region. When the charge segregation was disrupted, fusion pore opening was slowed, whereas docking was unchanged. Intramolecular disulfide cross-linking between N- and C-terminal regions of the linker or deletion of 40 residues from the linker reduced docking while enhancing pore opening, although the changes were subtle. EPR analysis showed Ca2+-induced line broadening reflecting a conformational change in the linker region. Thus the results of the present study suggest that the electrostatically bipartite linker region may extend for docking and fold to facilitate pore opening.

Indexed as

Membrane FusionAnimalsCalciumCations, DivalentCross-Linking ReagentsDisulfidesLipidsMembranes, ArtificialMutagenesis, Site-DirectedProtein ConformationRatsSNARE ProteinsStatic ElectricitySynaptic VesiclesSynaptotagmin ICalciumCations, DivalentCross-Linking ReagentsDisulfidesLipidsMembranes, ArtificialSNARE ProteinsSynaptotagmin I

Identifiers

PMID24001110
PMCPMC4418238

What OpenQuestion holds

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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.