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Medientyp:
E-Artikel
Titel:
Structural determinants of CO2-sensitivity in the β connexin family suggested by evolutionary analysis
Beteiligte:
Dospinescu, Valentin-Mihai;
Nijjar, Sarbjit;
Spanos, Fokion;
Cook, Jonathan;
de Wolf, Elizabeth;
Biscotti, Maria Assunta;
Gerdol, Marco;
Dale, Nicholas
Erschienen:
Springer Science and Business Media LLC, 2019
Erschienen in:Communications Biology
Sprache:
Englisch
DOI:
10.1038/s42003-019-0576-2
ISSN:
2399-3642
Entstehung:
Anmerkungen:
Beschreibung:
<jats:title>Abstract</jats:title><jats:p>A subclade of connexins comprising Cx26, Cx30, and Cx32 are directly sensitive to CO<jats:sub>2</jats:sub>. CO<jats:sub>2</jats:sub> binds to a carbamylation motif present in these connexins and causes their hemichannels to open. Cx26 may contribute to CO<jats:sub>2</jats:sub>-dependent regulation of breathing in mammals. Here, we show that the carbamylation motif occurs in a wide range of non-mammalian vertebrates and was likely present in the ancestor of all gnathostomes. While the carbamylation motif is essential for connexin CO<jats:sub>2</jats:sub>-sensitivity, it is not sufficient. In Cx26 of amphibia and lungfish, an extended C-terminal tail prevents CO<jats:sub>2</jats:sub>-evoked hemichannel opening despite the presence of the motif. Although Cx32 has a long C-terminal tail, Cx32 hemichannels open to CO<jats:sub>2</jats:sub> because the tail is conformationally restricted by the presence of proline residues. The loss of the C-terminal tail of Cx26 in amniotes was an evolutionary innovation that created a connexin hemichannel with CO<jats:sub>2</jats:sub>-sensing properties suitable for the regulation of breathing.</jats:p>