Evidence map›Paper›PMID 26195798›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Structural elements that underlie Doc2β function during asynchronous synaptic transmission.

Renhao Xue, Jon D Gaffaney, Edwin R Chapman

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 29 citations in OpenAlex.

  1. Increased CA3 burst activity inbioRxiv : the preprint server for biology · 2026
    Article
  2. Article
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  5. Review
  6. Article
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  9. Article
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  11. Review
  12. The Role of Calmodulin vs. Synaptotagmin in Exocytosis.Frontiers in molecular neuroscience · 2021
    Review
  13. Doc2 Proteins Are Not Required for the Increased Spontaneous Release Rate in Synaptotagmin-1-Deficient Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  14. Doc2b CaScientific reports · 2019
    Article
  15. The Ever-Growing Puzzle of Asynchronous Release.Frontiers in cellular neuroscience · 2019
    Review
  16. Doc2-mediated superpriming supports synaptic augmentation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. Article
  18. Review
  19. Article
  20. 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

3 authors at 2 institutions in 1 country.

Renhao XueDepartment of Neuroscience, University of Wisconsin, Madison, WI 53706; and Howard Hughes Medical Institute, University of Wisconsin, Madison, WI 53706.
Jon D GaffaneyDepartment of Neuroscience, University of Wisconsin, Madison, WI 53706; and Howard Hughes Medical Institute, University of Wisconsin, Madison, WI 53706.
Edwin R ChapmanDepartment of Neuroscience, University of Wisconsin, Madison, WI 53706; and Howard Hughes Medical Institute, University of Wisconsin, Madison, WI 53706 chapman@wisc.edu.
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 InstituteNIMH NIH HHS MH 61876NIMH NIH HHS R01 MH061876
6 · The paper itself

Abstract

Double C2-like domain-containing proteins alpha and beta (Doc2α and Doc2β) are tandem C2-domain proteins proposed to function as Ca(2+) sensors for asynchronous neurotransmitter release. Here, we systematically analyze each of the negatively charged residues that mediate binding of Ca(2+) to the β isoform. The Ca(2+) ligands in the C2A domain were dispensable for Ca(2+)-dependent translocation to the plasma membrane, with one exception: neutralization of D220 resulted in constitutive translocation. In contrast, three of the five Ca(2+) ligands in the C2B domain are required for translocation. Importantly, translocation was correlated with the ability of the mutants to enhance asynchronous release when overexpressed in neurons. Finally, replacement of specific Ca(2+)/lipid-binding loops of synaptotagmin 1, a Ca(2+) sensor for synchronous release, with corresponding loops from Doc2β, resulted in chimeras that yielded slower kinetics in vitro and slower excitatory postsynaptic current decays in neurons. Together, these data reveal the key determinants of Doc2β that underlie its function during the slow phase of synaptic transmission.

Indexed as

Synaptic TransmissionAnimalsCalciumCalcium-Binding ProteinsCell MembraneExcitatory Postsynaptic PotentialsGreen Fluorescent ProteinsHippocampusKineticsLigandsMembrane FusionMice, KnockoutMutant ProteinsMutationNerve Tissue ProteinsNeuronsCalciumCalcium-Binding ProteinsDoc2b protein, ratGreen Fluorescent ProteinsLigandsMutant ProteinsNerve Tissue ProteinsSNARE ProteinsSynaptotagmin Iasynchronous synaptic transmissionC2-domainCa2+ sensorDoc2βsynaptotagmin 1

Identifiers

PMID26195798
PMCPMC4534243
OpenAlexW1871478100

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.