Evidence map›Paper›PMID 18685021›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2008

Multiple RIBEYE-RIBEYE interactions create a dynamic scaffold for the formation of synaptic ribbons.

Venkat Giri Magupalli, Karin Schwarz, Kannan Alpadi, Sivaraman Natarajan, Gail M Seigel, Frank Schmitz

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

83 citing papers in PubMed, 166 citations in OpenAlex.

  1. Article
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  8. Review
  9. Recurrent connectivity supports carbon dioxide sensitivity inbioRxiv : the preprint server for biology · 2025
    Article
  10. Article
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  12. The Astrocytic Zinc Transporter ZIP12 Is a Synaptic Protein That Contributes to Synaptic Zinc Levels in the Mouse Auditory Cortex.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  13. Review
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  15. Article
  16. Article
  17. Role of Ribeye PXDLS/T-binding cleft in normal synaptic ribbon function.bioRxiv : the preprint server for biology · 2023
    Article
  18. Article
  19. Article
  20. Article

23 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

6 authors at 2 institutions in 2 countries.

Venkat Giri MagupalliDepartment of Neuroanatomy, Institute for Anatomy and Cell Biology, Saarland University, Medical School Homburg/Saar, 66421 Homburg/Saar, Germany.
Karin Schwarz
Kannan Alpadi
Sivaraman Natarajan
Gail M Seigel
Frank Schmitz
Saarland University · DEUniversity at Buffalo, State University of New York · US

Funding

UB VISION INFRASTRUCTURE CENTERR24EY016662 · NEI · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI GONZALEZ-FERNANDEZ, FEDERICO · 2005 to 2009
$989k
NEI NIH HHS R24 EY016662NEI NIH HHS R24EY016662
6 · The paper itself

Abstract

Synaptic ribbons are large, dynamic structures in the active zone complex of ribbon synapses and important for the physiological properties of these tonically active synapses. RIBEYE is a unique and major protein component of synaptic ribbons. The aim of the present study was to understand how the synaptic ribbon is built and how the construction of the ribbon could contribute to its ultrastructural plasticity. In the present study, we demonstrate that RIBEYE self-associates using different independent approaches (yeast two-hybrid analyses, protein pull downs, synaptic ribbon-RIBEYE interaction assays, coaggregation experiments, transmission electron microscopy and immunogold electron microscopy). The A-domain [RIBEYE(A)] and B-domain [RIBEYE(B)] of RIBEYE contain five distinct sites for RIBEYE-RIBEYE interactions. Three interaction sites are present in the A-domain of RIBEYE and mediate RIBEYE(A)-RIBEYE(A) homodimerization and heterodimerization with the B-domain. The docking site for RIBEYE(A) on RIBEYE(B) is topographically and functionally different from the RIBEYE(B) homodimerization interface and is negatively regulated by nicotinamide adenine dinucleotide. The identified multiple RIBEYE-RIBEYE interactions have the potential to build the synaptic ribbon: heterologously expressed RIBEYE forms large electron-dense aggregates that are in part physically associated with surrounding vesicles and membrane compartments. These structures resemble spherical synaptic ribbons. These ribbon-like structures coassemble with the active zone protein bassoon, an interaction partner of RIBEYE at the active zone of ribbon synapses, emphasizing the physiological relevance of these RIBEYE-containing aggregates. Based on the identified multiple RIBEYE-RIBEYE interactions, we provide a molecular mechanism for the dynamic assembly of synaptic ribbons from individual RIBEYE subunits.

Indexed as

Alcohol OxidoreductasesAnimalsBacteriaCell LineChlorocebus aethiopsCo-Repressor ProteinsCOS CellsDimerizationImmunohistochemistryMicroscopy, ElectronNADNerve Tissue ProteinsPichiaProtein IsoformsProtein Structure, TertiaryRetinaAlcohol OxidoreductasesBSN protein, humanCo-Repressor ProteinsCTBP2 protein, humanNADNerve Tissue ProteinsProtein Isoforms

Identifiers

PMID18685021
PMCPMC6670776
OpenAlexW1964650181

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.