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Cysteine residues in the cytoplasmic carboxy terminus of connexins dictate gap junction plaque stability
Gap junctions are cellular contact sites composed of clustered connexin transmembrane proteins that act in dual capacities as channels for direct intercellular exchange of small molecules and as structural adhesion complexes known as gap junction nexuses. Depending on the connexin isoform, the clust...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5638580/ https://www.ncbi.nlm.nih.gov/pubmed/28835376 http://dx.doi.org/10.1091/mbc.E17-03-0206 |
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author | Stout, Randy F. Spray, David C. |
author_facet | Stout, Randy F. Spray, David C. |
author_sort | Stout, Randy F. |
collection | PubMed |
description | Gap junctions are cellular contact sites composed of clustered connexin transmembrane proteins that act in dual capacities as channels for direct intercellular exchange of small molecules and as structural adhesion complexes known as gap junction nexuses. Depending on the connexin isoform, the cluster of channels (the gap junction plaque) can be stably or fluidly arranged. Here we used confocal microscopy and mutational analysis to identify the residues within the connexin proteins that determine gap junction plaque stability. We found that stability is altered by changing redox balance using a reducing agent—indicating gap junction nexus stability is modifiable. Stability of the arrangement of connexins is thought to regulate intercellular communication by establishing an ordered supramolecular platform. By identifying the residues that establish plaque stability, these studies lay the groundwork for exploration of mechanisms by which gap junction nexus stability modulates intercellular communication. |
format | Online Article Text |
id | pubmed-5638580 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-56385802017-12-30 Cysteine residues in the cytoplasmic carboxy terminus of connexins dictate gap junction plaque stability Stout, Randy F. Spray, David C. Mol Biol Cell Brief Reports Gap junctions are cellular contact sites composed of clustered connexin transmembrane proteins that act in dual capacities as channels for direct intercellular exchange of small molecules and as structural adhesion complexes known as gap junction nexuses. Depending on the connexin isoform, the cluster of channels (the gap junction plaque) can be stably or fluidly arranged. Here we used confocal microscopy and mutational analysis to identify the residues within the connexin proteins that determine gap junction plaque stability. We found that stability is altered by changing redox balance using a reducing agent—indicating gap junction nexus stability is modifiable. Stability of the arrangement of connexins is thought to regulate intercellular communication by establishing an ordered supramolecular platform. By identifying the residues that establish plaque stability, these studies lay the groundwork for exploration of mechanisms by which gap junction nexus stability modulates intercellular communication. The American Society for Cell Biology 2017-10-15 /pmc/articles/PMC5638580/ /pubmed/28835376 http://dx.doi.org/10.1091/mbc.E17-03-0206 Text en © 2017 Stout and Spray. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Brief Reports Stout, Randy F. Spray, David C. Cysteine residues in the cytoplasmic carboxy terminus of connexins dictate gap junction plaque stability |
title | Cysteine residues in the cytoplasmic carboxy terminus of connexins dictate gap junction plaque stability |
title_full | Cysteine residues in the cytoplasmic carboxy terminus of connexins dictate gap junction plaque stability |
title_fullStr | Cysteine residues in the cytoplasmic carboxy terminus of connexins dictate gap junction plaque stability |
title_full_unstemmed | Cysteine residues in the cytoplasmic carboxy terminus of connexins dictate gap junction plaque stability |
title_short | Cysteine residues in the cytoplasmic carboxy terminus of connexins dictate gap junction plaque stability |
title_sort | cysteine residues in the cytoplasmic carboxy terminus of connexins dictate gap junction plaque stability |
topic | Brief Reports |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5638580/ https://www.ncbi.nlm.nih.gov/pubmed/28835376 http://dx.doi.org/10.1091/mbc.E17-03-0206 |
work_keys_str_mv | AT stoutrandyf cysteineresiduesinthecytoplasmiccarboxyterminusofconnexinsdictategapjunctionplaquestability AT spraydavidc cysteineresiduesinthecytoplasmiccarboxyterminusofconnexinsdictategapjunctionplaquestability |