Evidence map›Paper›PMID 24133139›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Fast structural responses of gap junction membrane domains to AB5 toxins.

Irina V Majoul, Liang Gao, Eric Betzig, Daria Onichtchouk, Eugenia Butkevich, Yuri Kozlov, Feliksas Bukauskas, Michael V L Bennett, Jennifer Lippincott-Schwartz, Rainer Duden

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

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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

10 authors at 8 institutions in 3 countries.

Irina V MajoulInstitute of Biology, Center for Structural and Cell Biology in Medicine, University of Lübeck, 23562 Lübeck, Germany.
Liang Gao
Eric Betzig
Daria Onichtchouk
Eugenia Butkevich
Yuri Kozlov
Feliksas Bukauskas
Michael V L Bennett
Jennifer Lippincott-Schwartz
Rainer Duden
Albert Einstein College of Medicine · USUniversity of Lübeck · DEHoward Hughes Medical Institute · USJanelia Research Campus · USNational Institutes of Health · USRussian Academy of Sciences · RUUniversity of Freiburg · DEUniversity of Göttingen · DE

Funding

Organization and Dynamics of Endomembrane Pathways and OrganellesZIAHD001609 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BONIFACINO, JUAN · 2009 to 2019
$16.2M
Connexins and Heart FunctionR01HL084464 · NHLBI · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI BUKAUSKAS, FELIKSAS · 2007 to 2010
$1.7M
Cx43 Hemichannels: Gating, Modification and FunctionR01NS055363 · NINDS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI BENNETT, MICHAEL V L · 2007 to 2011
$1.6M
Gating of Connexin-Based Gap Junction Channels and HemichannelsR01NS072238 · NINDS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI BUKAUSKAS, FELIKSAS · 2010 to 2013
$1.4M
Howard Hughes Medical InstituteNHLBI NIH HHS HL84464NHLBI NIH HHS R01 HL084464NINDS NIH HHS NS55363NINDS NIH HHS NS72238NINDS NIH HHS R01 NS055363NINDS NIH HHS R01 NS072238
6 · The paper itself

Abstract

Gap junctions (GJs) represent connexin-rich membrane domains that connect interiors of adjoining cells in mammalian tissues. How fast GJs can respond to bacterial pathogens has not been known previously. Using Bessel beam plane illumination and confocal spinning disk microscopy, we found fast (~500 ms) formation of connexin-depleted regions (CDRs) inside GJ plaques between cells exposed to AB5 toxins. CDR formation appears as a fast redistribution of connexin channels within GJ plaques with minor changes in outline or geometry. CDR formation does not depend on membrane trafficking or submembrane cytoskeleton and has no effect on GJ conductance. However, CDR responses depend on membrane lipids, can be modified by cholesterol-clustering agents and extracellular K(+) ion concentration, and influence cAMP signaling. The CDR response of GJ plaques to bacterial toxins is a phenomenon observed for all tested connexin isoforms. Through signaling, the CDR response may enable cells to sense exposure to AB5 toxins. CDR formation may reflect lipid-phase separation events in the biological membrane of the GJ plaque, leading to increased connexin packing and lipid reorganization. Our data demonstrate very fast dynamics (in the millisecond-to-second range) within GJ plaques, which previously were considered to be relatively stable, long-lived structures.

Indexed as

Analysis of VarianceAnimalsBacterial ToxinsBridged Bicyclo Compounds, HeterocyclicChlorocebus aethiopsConnexinsCyclic AMPDNA PrimersFilipinFluorescenceGap JunctionsImage Processing, Computer-AssistedMembrane LipidsMicroscopy, ConfocalPatch-Clamp TechniquesPotassiumBacterial ToxinsBridged Bicyclo Compounds, HeterocyclicConnexinsCyclic AMPDNA PrimersFilipinlatrunculin AMembrane LipidsPotassiumThiazolidinescell–cell junctionscholesterolconnexin actinmembrane traffic

Identifiers

PMID24133139
PMCPMC3816413
OpenAlexW2087267500

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.