Evidence map›Paper›PMID 21179232›Full record

ArticleMolecular vision2010

Stability of active zone components at the photoreceptor ribbon complex.

Hanna Regus-Leidig, Dana Specht, Susanne Tom Dieck, Johann Helmut Brandstätter

Abstract read
In one paragraph

Article in Molecular vision, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. A non-conducting role of the CabioRxiv : the preprint server for biology · 2024
    Article
  6. Article
  7. Calcium Channels in Retinal Function and Disease.Annual review of vision science · 2022
    Review
  8. Article
  9. Impaired CaInternational journal of molecular sciences · 2021
    Article
  10. Review
  11. Article
  12. αThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  13. Analysis of RIM Expression and Function at Mouse Photoreceptor Ribbon Synapses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  14. Article
  15. Article
  16. Review
  17. RIM1/2-Mediated Facilitation of Cav1.4 Channel Opening Is Required for Ca2+-Stimulated Release in Mouse Rod Photoreceptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  18. Article
  19. Review
  20. Article
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.

Hanna Regus-LeidigDepartment of Biology, Animal Physiology, University of Erlangen-Nuremberg, Erlangen, Germany.
Dana Specht
Susanne Tom Dieck
Johann Helmut Brandstätter

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposePhotoreceptor ribbon synapses translate light-dependent changes of membrane potential into graded transmitter release over several orders of magnitude in intensity. A specialized organelle at the active zone--the synaptic ribbon--is a key player in this process, and it is well known that the ribbon undergoes illumination and thus activity-dependent structural changes. However, the molecular basis for these changes is unknown. The aim of this study was to correlate the known ultrastructural ribbon changes to the distribution of proteins of the presynaptic ribbon complex.

methodsIn an in vitro assay, two distinct structural ribbon states--club-shaped and spherical-shaped--were enriched and the distribution of presynaptic proteins at the rod photoreceptor ribbon complex was analyzed with immunocytochemistry and light and electron microscopy.

resultsWe show that structural changes of the ribbon correlate with the redistribution of selected presynaptic proteins. The disassembly of the ribbon complex seems to be a multistep process, which starts with the removal of spherical ribbon material while arciform density and active zone plasma membrane proteins remain largely unchanged at their synaptic location. Only later, in a second phase following the removal of ribbon material, the arciform density and plasma membrane proteins are redistributed from their synaptic localization and active zones disappear.

conclusionsThe results of our study show that photoreceptor ribbon and arciform density/plasma membrane components might be influenced differentially by activity-driven processes, thus providing a molecular basis for further investigation of regulatory and adaptive processes in photoreceptor ribbon synaptic transmission.

Indexed as

Alcohol OxidoreductasesAnimalsCell MembraneCo-Repressor ProteinsDNA-Binding ProteinsEgtazic AcidMembrane ProteinsMiceMice, Inbred C57BLNerve Tissue ProteinsPhosphoproteinsPhotoreceptor Cells, VertebrateRetinal Rod Photoreceptor CellsSynapsesAlcohol OxidoreductasesBsn protein, mouseCo-Repressor ProteinsCtbp2 protein, mouseDNA-Binding ProteinsEgtazic AcidMembrane ProteinsNerve Tissue ProteinsPhosphoproteins

Identifiers

PMID21179232
PMCPMC3002953

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Registered trials

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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.