Evidence map›Paper›PMID 23712261›Full record

ArticleThe Journal of cell biology2013

Cryo-electron tomography reveals a critical role of RIM1α in synaptic vesicle tethering.

Rubén Fernández-Busnadiego, Shoh Asano, Ana-Maria Oprisoreanu, Eri Sakata, Michael Doengi, Zdravko Kochovski, Magdalena Zürner, Valentin Stein, Susanne Schoch, Wolfgang Baumeister and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

85 citing papers in PubMed, 134 citations in OpenAlex.

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  15. Nanoscale architecture of synaptic vesicles and scaffolding complexes revealed by cryo-electron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2024
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25 more citing papers are in PubMed but not listed here.

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

11 authors at 2 institutions in 1 country.

Rubén Fernández-BusnadiegoDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Shoh Asano
Ana-Maria Oprisoreanu
Eri Sakata
Michael Doengi
Zdravko Kochovski
Magdalena Zürner
Valentin Stein
Susanne Schoch
Wolfgang Baumeister
Vladan Lucić
Max Planck Institute of Biochemistry · DEUniversity of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synaptic vesicles are embedded in a complex filamentous network at the presynaptic terminal. Before fusion, vesicles are linked to the active zone (AZ) by short filaments (tethers). The identity of the molecules that form and regulate tethers remains unknown, but Rab3-interacting molecule (RIM) is a prominent candidate, given its central role in AZ organization. In this paper, we analyzed presynaptic architecture of RIM1α knockout (KO) mice by cryo-electron tomography. In stark contrast to previous work on dehydrated, chemically fixed samples, our data show significant alterations in vesicle distribution and AZ tethering that could provide a structural basis for the functional deficits of RIM1α KO synapses. Proteasome inhibition reversed these structural defects, suggesting a functional recovery confirmed by electrophysiological recordings. Altogether, our results not only point to the ubiquitin-proteasome system as an important regulator of presynaptic architecture and function but also show that the tethering machinery plays a critical role in exocytosis, converging into a structural model of synaptic vesicle priming by RIM1α.

Indexed as

AnimalsExocytosisGTP-Binding ProteinsLeupeptinsMembrane FusionMiceMice, KnockoutProteasome Endopeptidase ComplexProteasome InhibitorsSynaptic VesiclesTomographybenzyloxycarbonylleucyl-leucyl-leucine aldehydeGTP-Binding ProteinsLeupeptinsProteasome Endopeptidase ComplexProteasome InhibitorsRims1 protein, mouse

Identifiers

PMID23712261
PMCPMC3664715
OpenAlexW2010816302

What OpenQuestion holds

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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.