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ciało-człowieka: Tunicate
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3 zapisanych źródełEvidence: 100 • authority: 72
Tunicates are marine invertebrates belonging to the subphylum Tunicata ( TEW-nih-KAY-tə). This grouping is part of the Chordata, a phylum which includes all animals with dorsal nerve cords and notochords (including vertebrates). The subphylum was at one time called Urochordata, and the term urochordates is still sometimes used for these animals. Despite their simple appearance and very different adult form, their close relationship to the vertebrates is certain. Both groups are chordates, as evidenced by the fact that during their mobile larval stage, tunicates possess a notochord, a hollow dorsal nerve cord, pharyngeal slits, post-anal tail, and an endostyle. They resemble a tadpole. Tunic…
Otwórz źródło ↗Evidence: 41 • authority: 88
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 Non-chordates use the primordial innexins, while chordates use connexins that superseded the gap junction function of innexins.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 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 gl…
Otwórz źródło ↗Evidence: 41 • authority: 88
Connexins evolved after early chordates lost innexin diversity. 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 Non-chordates use the primordial innexins, while chordates use connexins that superseded the gap junction function of innexins.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 2270 innexins from 152 non-chordate and 274 chordate species. Among all chordates, we found not a single innexin w…
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