Evidence map›Paper›PMID 22270918›Full record

ArticleThe Journal of cell biology2012

The synaptic vesicle SNARE neuronal Synaptobrevin promotes endolysosomal degradation and prevents neurodegeneration.

Adam Haberman, W Ryan Williamson, Daniel Epstein, Dong Wang, Srisha Rina, Ian A Meinertzhagen, P Robin Hiesinger

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
2.4field-weighted citation impact, top 12% 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

36 citing papers in PubMed, 1 synthesis or guideline pooled it, 50 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. microPublication biology · 2025
    Article
  5. Article
  6. Article
  7. Frontiers in aging neuroscience · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Autophagy and the endolysosomal system in presynaptic function.Cellular and molecular life sciences : CMLS · 2021
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

7 authors at 3 institutions in 3 countries.

Adam HabermanDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
W Ryan Williamson
Daniel Epstein
Dong Wang
Srisha Rina
Ian A Meinertzhagen
P Robin Hiesinger
The University of Texas Southwestern Medical Center · USCenter for Systems Biology · USNeuroscience Institute · IT

Funding

Regulation of Synaptic Specificity in the Visual System by Intracellular TraffickR01EY018884 · NEI · UT SOUTHWESTERN MEDICAL CENTER · PI HIESINGER, PETER ROBIN · 2008 to 2018
$3.6M
Visual system synapses and circuitsR01EY003592 · NEI · DALHOUSIE UNIVERSITY · PI MEINERTZHAGEN, IAN A · 1985 to 2013
$2.8M
NEI NIH HHS R01 EY003592NEI NIH HHS R01 EY018884NEI NIH HHS R01EY018884NEI NIH HHS R01EY03592
6 · The paper itself

Abstract

Soluble NSF attachment protein receptors (SNAREs) are the core proteins in membrane fusion. The neuron-specific synaptic v-SNARE n-syb (neuronal Synaptobrevin) plays a key role during synaptic vesicle exocytosis. In this paper, we report that loss of n-syb caused slow neurodegeneration independent of its role in neurotransmitter release in adult Drosophila melanogaster photoreceptor neurons. In addition to synaptic vesicles, n-Syb localized to endosomal vesicles. Loss of n-syb lead to endosomal accumulations, transmembrane protein degradation defects, and a secondary increase in autophagy. Our evidence suggests a primary defect of impaired delivery of vesicles that contain degradation proteins, including the acidification-activated Cathepsin proteases and the neuron-specific proton pump and V0 adenosine triphosphatase component V100. Overexpressing V100 partially rescued n-syb-dependent degeneration through an acidification-independent endosomal sorting mechanism. Collectively, these findings reveal a role for n-Syb in a neuron-specific sort-and-degrade mechanism that protects neurons from degeneration. Our findings further shed light on which intraneuronal compartments exhibit increased or decreased neurotoxicity.

Indexed as

AnimalsDrosophila melanogasterDrosophila ProteinsEndosomesLysosomesNeuronsProteolysisR-SNARE ProteinsSynaptic VesiclesVacuolar Proton-Translocating ATPasesDrosophila Proteinsnsyb protein, DrosophilaR-SNARE ProteinsVacuolar Proton-Translocating ATPasesVha100-1 protein, Drosophila

Identifiers

PMID22270918
PMCPMC3265959
OpenAlexW2154852038

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.