The vertebrate Aqp14 water channel is a neuropeptide-regulated polytransporter

• Published in: Communications Biology
• Main Authors: Chauvigné, François, Yilmaz, Ozlem, Ferré, Alba, Fjelldal, Per Gunnar, Finn, Roderick N., Cerdà, Joan
• Other Authors: Ministerio de Economía y Competitividad (España), Norwegian Research Council
• Format: Article in Journal/Newspaper
• Language: English
• Published: Nature Publishing Group 2019
• Subjects: Atlantic salmon
• Online Access: http://hdl.handle.net/10261/342669; https://doi.org/10.1038/s42003-019-0713-y

13 pages, 7 figures, supplementary information https://doi.org/10.1038/s42003-019-0713-y.-- Data availability: The nucleotide sequences corresponding to the aqp14 cDNAs from gilthead seabream, zebrafish and Atlantic salmon were deposited in GenBank with accession numbers MK883753, MK883754 and MK883755, respectively. All data generated or analysed during this study are included in this published article (and its supplementary information files).-- Data availability: The nucleotide sequences corresponding to the aqp14 cDNAs from gilthead seabream, zebrafish and Atlantic salmon were deposited in GenBank with accession numbers MK883753, MK883754 and MK883755, respectively. All data generated or analysed during this study are included in this published article (and its supplementary information files) Water channels (aquaporins) were originally discovered in mammals with fourteen subfamilies now identified (AQP0-13). Here we show that a functional Aqp14 subfamily phylogenetically related to AQP4-type channels exists in all vertebrate lineages except hagfishes and eutherian mammals. In contrast to the water-selective classical aquaporins, which have four aromatic-arginine constriction residues, Aqp14 proteins present five non-aromatic constriction residues and facilitate the permeation of water, urea, ammonia, H2O2 and glycerol. Immunocytochemical assays suggest that Aqp14 channels play important osmoregulatory roles in piscine seawater adaptation. Our data indicate that Aqp14 intracellular trafficking is tightly regulated by the vasotocinergic/isotocinergic neuropeptide and receptor systems, whereby protein kinase C and A transduction pathways phosphorylate highly conserved C-terminal residues to control channel plasma membrane insertion. The neuropeptide regulation of Aqp14 channels thus predates the vasotocin/vasopressin regulation of AQP2-5-6 orthologs observed in tetrapods. These findings demonstrate that vertebrate Aqp14 channels represent an ancient subfamily of neuropeptide-regulated polytransporters This ...