Evidence map›Paper›PMID 27115346›Full record

ArticleeLife2016

Analysis of protein phosphorylation in nerve terminal reveals extensive changes in active zone proteins upon exocytosis.

Mahdokht Kohansal-Nodehi, John Je Chua, Henning Urlaub, Reinhard Jahn, Dominika Czernik

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. 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
3.2field-weighted citation impact, top 9% 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, 62 citations in OpenAlex.

  1. Active zone plasticity couples sleep need to presynaptic hypophosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  8. Syntaxin 3B: A SNARE Protein Required for Vision.International journal of molecular sciences · 2024
    Review
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  16. Presynaptic Short-Term Plasticity Persists in the Absence of PKC Phosphorylation of Munc18-1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
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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 at 3 institutions in 2 countries.

Mahdokht Kohansal-NodehiDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0002-3898-5197
John Je ChuaInteractomics and Intracellular Trafficking laboratory, National University of Singapore, Singapore, Singapore.ORCID 0000-0002-5615-1014
Henning UrlaubBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Reinhard JahnDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0003-1542-3498
Dominika CzernikDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0001-7911-0867
Max Planck Institute for Biophysical Chemistry · DENational University of Singapore · SGUniversitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurotransmitter release is mediated by the fast, calcium-triggered fusion of synaptic vesicles with the presynaptic plasma membrane, followed by endocytosis and recycling of the membrane of synaptic vesicles. While many of the proteins governing these processes are known, their regulation is only beginning to be understood. Here we have applied quantitative phosphoproteomics to identify changes in phosphorylation status of presynaptic proteins in resting and stimulated nerve terminals isolated from the brains of Wistar rats. Using rigorous quantification, we identified 252 phosphosites that are either up- or downregulated upon triggering calcium-dependent exocytosis. Particularly pronounced were regulated changes of phosphosites within protein constituents of the presynaptic active zone, including bassoon, piccolo, and RIM1. Additionally, we have mapped kinases and phosphatases that are activated upon stimulation. Overall, our study provides a snapshot of phosphorylation changes associated with presynaptic activity and provides a foundation for further functional analysis of key phosphosites involved in presynaptic plasticity.

Indexed as

ExocytosisProtein Processing, Post-TranslationalAnimalsBrainNeuronsPhosphorylationPresynaptic TerminalsProteinsProteomeRats, WistarProteinsProteomeactive zoneexocytosisneurosciencephosphoproteomicsphosphorylationprotein kinaseratsynaptosome

Identifiers

PMID27115346
PMCPMC4894758
OpenAlexW2344020670

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.