Evidence map›Paper›PMID 20573977›Full record

ArticleMolecular biology of the cell2010

Regulation of exocytosis and fusion pores by synaptotagmin-effector interactions.

Zhen Zhang, Enfu Hui, Edwin R Chapman, Meyer B Jackson

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

29 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  4. High-speed imaging reveals the bimodal nature of dense core vesicle exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Article
  6. Neuromodulator release in neurons requires two functionally redundant calcium sensors.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  18. An Engineered Metal Sensor Tunes the Kinetics of Synaptic Transmission.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    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

4 authors at 4 institutions in 1 country.

Zhen ZhangNational Institute of Neurological Disorders and Stroke, Bethesda, MD 20892, USA.
Enfu Hui
Edwin R Chapman
Meyer B Jackson
Howard Hughes Medical Institute · USNational Institute of Neurological Disorders and Stroke · USUniversity of California, San Francisco · USUniversity of Wisconsin–Madison · US

Funding

Synaptotagmin C2B Domain as a Ca2+ Sensing ModuleR01MH061876 · NIMH · UNIVERSITY OF WISCONSIN-MADISON · PI Edwin R Chapman · 2002 to 2026
$7.7M
Single-Channel Studies of the Fusion PoreR01NS044057 · NINDS · UNIVERSITY OF WISCONSIN-MADISON · PI JACKSON, MEYER B. · 2002 to 2022
$5.7M
Howard Hughes Medical InstituteNIMH NIH HHS MH61876NIMH NIH HHS R01 MH061876NINDS NIH HHS NS44057NINDS NIH HHS R01 NS044057
6 · The paper itself

Abstract

Synaptotagmin (syt) serves as a Ca(2+) sensor in the release of neurotransmitters and hormones. This function depends on the ability of syt to interact with other molecules. Syt binds to phosphatidylserine (PS)-containing lipid bilayers as well as to soluble N-ethylmaleimide sensitive factor receptors (SNAREs) and promotes SNARE assembly. All these interactions are regulated by Ca(2+), but their specific roles in distinct kinetic steps of exocytosis are not well understood. To explore these questions we used amperometry recording from PC12 cells to investigate the kinetics of exocytosis. Syt isoforms and syt I mutants were overexpressed to perturb syt-PS and syt-SNARE interactions to varying degrees and evaluate the effects on fusion event frequency and the rates of fusion pore transitions. Syt I produced more rapid dilation of fusion pores than syt VII or syt IX, consistent with its role in synchronous synaptic release. Stronger syt-PS interactions were accompanied by a higher frequency of fusion events and more stable fusion pores. By contrast, syt-SNARE interactions and syt-induced SNARE assembly were uncorrelated with rates of exocytosis. This associates the syt-PS interaction with two distinct kinetic steps in Ca(2+) triggered exocytosis and supports a role for the syt-PS interaction in stabilizing open fusion pores.

Indexed as

Amino Acid SubstitutionAnimalsBlotting, WesternCalciumElectrochemical TechniquesExocytosisKineticsLipid BilayersMembrane FusionMutationPC12 CellsPhosphatidylserinesProtein BindingProtein IsoformsRatsSNARE ProteinsCalciumLipid BilayersPhosphatidylserinesProtein IsoformsSNARE ProteinsSynaptotagmin ISynaptotagmins

Identifiers

PMID20573977
PMCPMC2921110
OpenAlexW2106431604

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.