ArticleThe Biochemical journal2011
Different domains are critical for oligomerization compatibility of different connexins.
Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Cx43 enhances response to BRAF/MEK inhibitors by reducing DNA repair capacity.Nature communications · 2025Article
- Cx31.1 can selectively intermix with co-expressed connexins to facilitate its assembly into gap junctions.Journal of cell science · 2024Article
- Article
- Concatenation of Human Connexin26 (hCx26) and Human Connexin46 (hCx46) for the Analysis of Heteromeric Gap Junction Hemichannels and Heterotypic Gap Junction Channels.International journal of molecular sciences · 2018Article
- Accessing gap-junction channel structure-function relationships through molecular modeling and simulations.BMC cell biology · 2017Review
- Syndromic deafness mutations at Asn 14 differentially alter the open stability of Cx26 hemichannels.The Journal of general physiology · 2016Article
- Connexinopathies: a structural and functional glimpse.BMC cell biology · 2016Review
- Simvastatin Sodium Salt and Fluvastatin Interact with Human Gap Junction Gamma-3 Protein.PloS one · 2016Article
- Keratitis-ichthyosis-deafness syndrome-associated Cx26 mutants produce nonfunctional gap junctions but hyperactive hemichannels when co-expressed with wild type Cx43.The Journal of investigative dermatology · 2015Article
- Mix and match: investigating heteromeric and heterotypic gap junction channels in model systems and native tissues.FEBS letters · 2014Review
- Identification of a dimerization domain in the TMEM16A calcium-activated chloride channel (CaCC).Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Interfering amino terminal peptides and functional implications for heteromeric gap junction formation.Frontiers in pharmacology · 2013Article
- Critical role of the first transmembrane domain of Cx26 in regulating oligomerization and function.Molecular biology of the cell · 2012Article
- Cytoplasmic amino acids within the membrane interface region influence connexin oligomerization.The Journal of membrane biology · 2012Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Oligomerization of connexins is a critical step in gap junction channel formation. Some members of the connexin family can oligomerize with other members and form functional heteromeric hemichannels [e.g. Cx43 (connexin 43) and Cx45], but others are incompatible (e.g. Cx43 and Cx26). To find connexin domains important for oligomerization, we constructed chimaeras between Cx43 and Cx26 and studied their ability to oligomerize with wild-type Cx43, Cx45 or Cx26. HeLa cells co-expressing Cx43, Cx45 or Cx26 and individual chimaeric constructs were analysed for interactions between the chimaeras and the wild-type connexins using cell biological (subcellular localization by immunofluorescence), functional (intercellular diffusion of microinjected Lucifer yellow) and biochemical (sedimentation velocity through sucrose gradients) assays. All of the chimaeras containing the third transmembrane domain of Cx43 interacted with wild-type Cx43 on the basis of co-localization, dominant-negative inhibition of intercellular communication, and altered sedimentation velocity. The same chimaeras also interacted with co-expressed Cx45. In contrast, immunofluorescence and intracellular diffusion of tracer suggested that other domains influenced oligomerization compatibility when chimaeras were co-expressed with Cx26. Taken together, these results suggest that amino acids in the third transmembrane domain are critical for oligomerization with Cx43 and Cx45. However, motifs in different domains may determine oligomerization compatibility in members of different connexin subfamilies.
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