Evidence map›Paper›PMID 31557934›Full record

ArticleCells2019

Tubulin-Dependent Transport of Connexin-36 Potentiates the Size and Strength of Electrical Synapses.

Cherie A Brown, Cristiane Del Corsso, Christiane Zoidl, Logan W Donaldson, David C Spray, Georg Zoidl

Open access · goldAbstract read
In one paragraph

Article in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

12 citing papers in PubMed, 14 citations in OpenAlex.

  1. Defining the electrical synapse.Nature reviews. Neuroscience · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. The Roles of Calmodulin and CaMKII in Cx36 Plasticity.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Endocytosis of Connexin 36 is Mediated by Interaction with Caveolin-1.International journal of molecular sciences · 2020
    Article
  12. 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

6 authors at 3 institutions in 3 countries.

Cherie A BrownDepartment of Biology, York University, Toronto, ON M3J 1P3, Canada. cbrown88@yorku.ca.
Cristiane Del CorssoDepartment of Biophysics and Physiology, Federal University of Rio de Janeiro-RJ, Rio de Janeiro 21941-901, Brazil. cdcorsso@biof.ufrj.br.
Christiane ZoidlDepartment of Biology, York University, Toronto, ON M3J 1P3, Canada. czoidl@yorku.ca.
Logan W DonaldsonDepartment of Biology, York University, Toronto, ON M3J 1P3, Canada. logand@yorku.ca.
David C SprayDepartment of Neuroscience, Albert Einstein College, Bronx, NY 10461, USA. david.spray@einstein.yu.edu.
Georg ZoidlDepartment of Biology, York University, Toronto, ON M3J 1P3, Canada. gzoidl@yorku.ca.
York University · CAAlbert Einstein College of Medicine · USUniversidade Federal do Rio de Janeiro · BR

Funding

The Astrocyte Nexus: Cx43 Protein InteractionsR01NS092466 · NINDS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI SCEMES, ELIANA, SPRAY, DAVID C · 2015 to 2019
$2.6M
NINDS NIH HHS R01 NS092466
6 · The paper itself

Abstract

Connexin-36 (Cx36) electrical synapses strengthen transmission in a calcium/calmodulin (CaM)/calmodulin-dependent kinase II (CaMKII)-dependent manner similar to a mechanism whereby the N-methyl-D-aspartate (NMDA) receptor subunit NR2B facilitates chemical transmission. Since NR2B-microtubule interactions recruit receptors to the cell membrane during plasticity, we hypothesized an analogous modality for Cx36. We determined that Cx36 binding to tubulin at the carboxy-terminal domain was distinct from Cx43 and NR2B by binding a motif overlapping with the CaM and CaMKII binding motifs. Dual patch-clamp recordings demonstrated that pharmacological interference of the cytoskeleton and deleting the binding motif at the Cx36 carboxyl-terminal (CT) reversibly abolished Cx36 plasticity. Mechanistic details of trafficking to the gap-junction plaque (GJP) were probed pharmacologically and through mutational analysis, all of which affected GJP size and formation between cell pairs. Lys279, Ile280, and Lys281 positions were particularly critical. This study demonstrates that tubulin-dependent transport of Cx36 potentiates synaptic strength by delivering channels to GJPs, reinforcing the role of protein transport at chemical and electrical synapses to fine-tune communication between neurons.

Indexed as

AnimalsBiomechanical PhenomenaConnexinsElectrical SynapsesGap Junction delta-2 ProteinGap JunctionsMiceNeuronal PlasticityNeuronsProtein BindingProtein TransportRatsTubulinTumor Cells, CulturedConnexinsGap Junction delta-2 ProteinTubulinConnexin-36 (Cx36)cytoskeletonelectrical plasticitygap junctiontransporttubulin and microtubules

Identifiers

PMID31557934
PMCPMC6829524
OpenAlexW2975612455

What OpenQuestion 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 OpenQuestion graph.