Evidence map›Paper›PMID 18508778›Full record

ArticleThe Journal of biological chemistry2008

Analysis of the synaptotagmin family during reconstituted membrane fusion. Uncovering a class of inhibitory isoforms.

Akhil Bhalla, Michael C Chicka, Edwin R Chapman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.3field-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

52 citing papers in PubMed, 72 citations in OpenAlex.

  1. Alternative splicing of synaptotagmin 7 regulates oligomerization and short-term synaptic plasticity.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  5. Proper Frequency of Perinatal Retinal Waves Is Essential for the Precise Wiring of Visual Axons in Nonimage-Forming Nuclei.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
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  10. Synaptotagmin 9 Modulates Spontaneous Neurotransmitter Release in Striatal Neurons by Regulating Substance P Secretion.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
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  15. Neuromodulator release in neurons requires two functionally redundant calcium sensors.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  19. Phosphatidylinositol 4,5-bisphosphate drives CaThe Journal of biological chemistry · 2019
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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

3 authors at 2 institutions in 1 country.

Akhil BhallaHoward Hughes Medical Institute, and Department of Physiology, University of Wisconsin, 1300 University Avenue, Madison, WI 53706, USA.
Michael C Chicka
Edwin R Chapman
University of Wisconsin–Madison · USHoward 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 Institute
6 · The paper itself

Abstract

Ca(2+)-triggered exocytosis in neurons and neuroendocrine cells is regulated by the Ca(2+)-binding protein synaptotagmin (syt) I. Sixteen additional isoforms of syt have been identified, but little is known concerning their biochemical or functional properties. Here, we assessed the abilities of fourteen syt isoforms to directly regulate SNARE (soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor)-catalyzed membrane fusion. One group of isoforms stimulated neuronal SNARE-mediated fusion in response to Ca(2+), while another set inhibited SNARE catalyzed fusion in both the absence and presence of Ca(2+). Biochemical analysis revealed a strong correlation between the ability of syt isoforms to bind 1,2-dioleoyl phosphatidylserine (PS) and t-SNAREs in a Ca(2+)-promoted manner with their abilities to enhance fusion, further establishing PS and SNAREs as critical effectors for syt action. The ability of syt I to efficiently stimulate fusion was specific for certain SNARE pairs, suggesting that syts might contribute to the specificity of intracellular membrane fusion reactions. Finally, a subset of inhibitory syts down-regulated the ability of syt I to activate fusion, demonstrating that syt isoforms can modulate the function of each other.

Indexed as

Gene Expression RegulationAnimalsCalciumHumansMembrane FusionModels, BiologicalMolecular ConformationNeuronsPlasmidsProtein IsoformsProtein Structure, SecondaryProtein Structure, TertiaryRatsSNARE ProteinsSynaptotagminsCalciumProtein IsoformsSNARE ProteinsSynaptotagmins

Identifiers

PMID18508778
PMCPMC2490792
OpenAlexW2006221005

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.