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XB-ART-60448
Genome Biol Evol 2024 Jan 05;161:. doi: 10.1093/gbe/evad221.
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Functional divergence in solute permeability between ray-finned fish-specific paralogs of aqp10.

Imaizumi G , Ushio K , Nishihara H , Braasch I , Watanabe E , Kumagai S , Furuta T , Matsuzaki K , Romero MF , Kato A , Nagashima A .


Abstract
Aquaporin (Aqp) 10 is a member of the aquaglyceroporin subfamily of water channels, and human Aqp10 is permeable to solutes such as glycerol, urea, and boric acid. Tetrapods have a single aqp10 gene, whereas ray-finned fishes have paralogs of this gene through tandem duplication, whole-genome duplication, and subsequent deletion. A previous study on Aqps in the Japanese pufferfish Takifugu rubripes showed that one pufferfish paralog, Aqp10.2b, was permeable to water and glycerol, but not to urea and boric acid. To understand the functional differences of Aqp10 s between humans and pufferfish from an evolutionary perspective, we analyzed Aqp10 s from an amphibian (Xenopus laevis) and a lobe-finned fish (Protopterus annectens), and Aqp10.1 and Aqp10.2 from several ray-finned fishes (Polypterus senegalus, Lepisosteus oculatus, Danio rerio and Clupea pallasii). The expression of tetrapod and lobe-finned fish Aqp10 s and Aqp10.1-derived Aqps in ray-finned fishes in Xenopus oocytes increased the membrane permeabilities to water, glycerol, urea and boric acid. In contrast, Aqp10.2-derived Aqps in ray-finned fishes increased water and glycerol permeabilities, while those of urea and boric acid were much weaker than those of Aqp10.1-derived Aqps. These results indicate that water, glycerol, urea, and boric acid permeability are plesiomorphic activities of Aqp10 s, and that the ray-finned fish-specific Aqp10.2 paralogs have secondarily reduced or lost urea and boric acid permeability.

PubMed ID: 38039384
PMC ID: PMC10769510
Article link: Genome Biol Evol
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: actb aqp10 aqp3 aqp7 aqp8 aqp9 gars1
GO keywords: water channel activity


Article Images: [+] show captions
References [+] :
Agre, Aquaporin water channels--from atomic structure to clinical medicine. 2002, Pubmed