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Connexins evolved after early chordates lost innexin diversity.
- Source :
-
ELife [Elife] 2022 Jan 19; Vol. 11. Date of Electronic Publication: 2022 Jan 19. - Publication Year :
- 2022
-
Abstract
- 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 Non-chordates use the primordial innexins, while chordates use connexins that superseded the gap junction function of innexins.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.<br />Competing Interests: GW, SS No competing interests declared<br /> (© 2022, Welzel and Schuster.)
Details
- Language :
- English
- ISSN :
- 2050-084X
- Volume :
- 11
- Database :
- MEDLINE
- Journal :
- ELife
- Publication Type :
- Academic Journal
- Accession number :
- 35042580
- Full Text :
- https://doi.org/10.7554/eLife.74422