Connexins evolved after early chordates lost innexin diversity
Gap junction channels are formed by two unrelated protein families. Non-chordates use the primordial innexins, while chordates use connexins that superseded the gap junction function of innexins. Chordates retained innexin-homologs, but N-glycosylation prevents them from forming gap junctions. It is...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2022-01-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/74422 |
| _version_ | 1811201589798502400 |
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| author | Georg Welzel Stefan Schuster |
| author_facet | Georg Welzel Stefan Schuster |
| author_sort | Georg Welzel |
| collection | DOAJ |
| description | Gap junction channels are formed by two unrelated protein families. Non-chordates use the primordial innexins, while chordates use connexins that superseded the gap junction function of innexins. Chordates retained innexin-homologs, but N-glycosylation prevents them from forming gap junctions. It is puzzling why chordates seem to exclusively use the new gap junction protein and why no chordates should exist that use non-glycosylated innexins to form gap junctions. Here, we identified glycosylation sites of 2388 innexins from 174 non-chordate and 276 chordate species. Among all chordates, we found not a single innexin without glycosylation sites. Surprisingly, the glycosylation motif is also widespread among non-chordate innexins indicating that glycosylated innexins are not a novelty of chordates. In addition, we discovered a loss of innexin diversity during early chordate evolution. Most importantly, lancelets, which lack connexins, exclusively possess only one highly conserved innexin with one glycosylation site. A bottleneck effect might thus explain why connexins have become the only protein used to form chordate gap junctions. |
| first_indexed | 2024-04-12T02:24:12Z |
| format | Article |
| id | doaj.art-3ff6d3455cd5497d9561e70a1ab21830 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T02:24:12Z |
| publishDate | 2022-01-01 |
| publisher | eLife Sciences Publications Ltd |
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| series | eLife |
| spelling | doaj.art-3ff6d3455cd5497d9561e70a1ab218302022-12-22T03:52:02ZengeLife Sciences Publications LtdeLife2050-084X2022-01-011110.7554/eLife.74422Connexins evolved after early chordates lost innexin diversityGeorg Welzel0https://orcid.org/0000-0002-7017-604XStefan Schuster1https://orcid.org/0000-0002-0873-8996Department of Animal Physiology, University of Bayreuth, Bayreuth, GermanyDepartment of Animal Physiology, University of Bayreuth, Bayreuth, GermanyGap junction channels are formed by two unrelated protein families. Non-chordates use the primordial innexins, while chordates use connexins that superseded the gap junction function of innexins. Chordates retained innexin-homologs, but N-glycosylation prevents them from forming gap junctions. It is puzzling why chordates seem to exclusively use the new gap junction protein and why no chordates should exist that use non-glycosylated innexins to form gap junctions. Here, we identified glycosylation sites of 2388 innexins from 174 non-chordate and 276 chordate species. Among all chordates, we found not a single innexin without glycosylation sites. Surprisingly, the glycosylation motif is also widespread among non-chordate innexins indicating that glycosylated innexins are not a novelty of chordates. In addition, we discovered a loss of innexin diversity during early chordate evolution. Most importantly, lancelets, which lack connexins, exclusively possess only one highly conserved innexin with one glycosylation site. A bottleneck effect might thus explain why connexins have become the only protein used to form chordate gap junctions.https://elifesciences.org/articles/74422gap junction evolutioninnexinpannexinconnexinN-glycosylation |
| spellingShingle | Georg Welzel Stefan Schuster Connexins evolved after early chordates lost innexin diversity eLife gap junction evolution innexin pannexin connexin N-glycosylation |
| title | Connexins evolved after early chordates lost innexin diversity |
| title_full | Connexins evolved after early chordates lost innexin diversity |
| title_fullStr | Connexins evolved after early chordates lost innexin diversity |
| title_full_unstemmed | Connexins evolved after early chordates lost innexin diversity |
| title_short | Connexins evolved after early chordates lost innexin diversity |
| title_sort | connexins evolved after early chordates lost innexin diversity |
| topic | gap junction evolution innexin pannexin connexin N-glycosylation |
| url | https://elifesciences.org/articles/74422 |
| work_keys_str_mv | AT georgwelzel connexinsevolvedafterearlychordateslostinnexindiversity AT stefanschuster connexinsevolvedafterearlychordateslostinnexindiversity |