Evidence map›Paper›PMID 22722764›Full record

ArticleThe Journal of membrane biology2012

Under construction: building the macromolecular superstructure and signaling components of an electrical synapse.

B D Lynn, Xinbo Li, J I Nagy

Abstract read
In one paragraph

Article in The Journal of membrane biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

24 citing papers in PubMed, 39 citations in OpenAlex.

  1. Defining the electrical synapse.Nature reviews. Neuroscience · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. No tight junctions in tight junction protein-1 expressing HeLa and fibroblast cells.International journal of physiology, pathophysiology and pharmacology · 2020
    Article
  9. Connexin36 localization along axon initial segments in the mammalian CNS.International journal of physiology, pathophysiology and pharmacology · 2020
    Article
  10. ZO-1 associates with α3 integrin and connexin43 in trabecular meshwork and Schlemm's canal cells.International journal of physiology, pathophysiology and pharmacology · 2020
    Article
  11. Article
  12. Review
  13. Article
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  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
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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

3 authors at 2 institutions in 2 countries.

B D LynnDepartment of Physiology, Faculty of Medicine, University of Manitoba, Winnipeg, MB R3E 0J9, Canada.
Xinbo Li
J I Nagy
University of Manitoba · CAOregon Health & Science University · US

Funding

Connexins in Neuronal and Glial Gap Junctions in the Central Nervous SystemR01NS044395 · NINDS · COLORADO STATE UNIVERSITY-FORT COLLINS · PI RASH, JOHN E · 2002 to 2012
$3.5M
Gap Junctions and Connexins in Developing CNSR01NS044010 · NINDS · COLORADO STATE UNIVERSITY-FORT COLLINS · PI RASH, JOHN E · 2002 to 2005
$1.1M
Connexins in Neuronal and Glial Gap Junctions in the Central Nervous SystemR56NS044395 · NINDS · COLORADO STATE UNIVERSITY · PI RASH, JOHN E · 2007 to 2007
$360k
GAP JUNCTIONS IN IDENTIFIED SPINAL CORD NEURONSR01NS031027 · NINDS · COLORADO STATE UNIVERSITY-FORT COLLINS · PI RASH, JOHN E · 1994 to 1997
–
CIHR MOP 106598NINDS NIH HHS NS31027NINDS NIH HHS NS44010NINDS NIH HHS NS44395NINDS NIH HHS R01 NS044010NINDS NIH HHS R01 NS044395NINDS NIH HHS R56 NS044395
6 · The paper itself

Abstract

A great deal is now known about the protein components of tight junctions and adherens junctions, as well as how these are assembled. Less is known about the molecular framework of gap junctions, but these also have membrane specializations and are subject to regulation of their assembly and turnover. Thus, it is reasonable to consider that these three types of junctions may share macromolecular commonalities. Indeed, the tight junction scaffolding protein zonula occluden-1 (ZO-1) is also present at adherens and gap junctions, including neuronal gap junctions. On the basis of these earlier observations, we more recently found that two additional proteins, AF6 and MUPP1, known to be associated with ZO-1 at tight and adherens junctions, are also components of neuronal gap junctions in rodent brain and directly interact with connexin36 (Cx36) that forms these junctions. Here, we show by immunofluorescence labeling that the cytoskeletal-associated protein cingulin, commonly found at tight junctions, is also localized at neuronal gap junctions throughout the central nervous system. In consideration of known functions related to ZO-1, AF6, MUPP1, and cingulin, our results provide a context in which to examine functional relationships between these proteins at Cx36-containing electrical synapses in brain--specifically, how they may contribute to regulation of transmission at these synapses, and how they may govern gap junction channel assembly and/or disassembly.

Indexed as

AnimalsBrainCarrier ProteinsConnexinsElectrical SynapsesGap Junction delta-2 ProteinGap JunctionsImmunohistochemistryKinesinsMembrane ProteinsMiceMice, Inbred C57BLMultiprotein ComplexesMyosinsNeuronsZonula Occludens-1 ProteinAfdn protein, mouseCarrier ProteinsCgn protein, mouseConnexinsGap Junction delta-2 ProteinKinesinsMembrane ProteinsMpdz protein, mouseMultiprotein ComplexesMyosinsTjp1 protein, mouseZonula Occludens-1 Protein

Identifiers

PMID22722764
PMCPMC3506381
OpenAlexW2066321658

What OpenQuestion holds

Textmetadata
LicenceTDM
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.