ArticleProceedings of the National Academy of Sciences of the United States of America2013
Fast structural responses of gap junction membrane domains to AB5 toxins.
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.
What it found
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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.
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.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Current and future applications of light-sheet imaging for identifying molecular and developmental processes in autism spectrum disorders.Molecular psychiatry · 2024Review
- The dynamic Nexus: gap junctions control protein localization and mobility in distinct and surprising ways.Scientific reports · 2020Article
- Spatio-temporal regulation of connexin43 phosphorylation and gap junction dynamics.Biochimica et biophysica acta. Biomembranes · 2018Review
- Real-time investigation of dynamic protein crystallization in living cells.Structural dynamics (Melville, N.Y.) · 2015Article
- 3D live fluorescence imaging of cellular dynamics using Bessel beam plane illumination microscopy.Nature protocols · 2014Article
- Trafficking highways to the intercalated disc: new insights unlocking the specificity of connexin 43 localization.Cell communication & adhesion · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 8 institutions in 3 countries.
Funding
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.
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Registered trials
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.