Aquaporin Evolution in Fishes

Finn, Roderick Nigel; Cerdà, Joan

doi:10.3389/fphys.2011.00044

Cited by 55 publications

(41 citation statements)

References 56 publications

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“…As shown in S1 Fig, all Aqps possess one conserved domain (MIP) except for Aqp8ab-2, which is consistent with previous reports on Aqp protein structure [21], indicating high conservation of aqp s. Additionally, there are four Aqps (Aqp7-2, 11b-1, 11b-2 and 15–2) contain the transmembrane domain (TM) at the N-terminal or C-terminal end of the protein, and eight Aqps (Aqp3b-1, 3b-2, 4b-1, 8ab-2, 9a-1, 9a-2, 10a-1 and 10a-2) exhibited low complexity (LW) in the domain structure prediction.…”

Section: Resultssupporting

confidence: 91%

Genome Wide Identification, Phylogeny, and Expression of Aquaporin Genes in Common Carp (Cyprinus carpio)

et al. 2016

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BackgroundAquaporins (Aqps) are integral membrane proteins that facilitate the transport of water and small solutes across cell membranes. Among vertebrate species, Aqps are highly conserved in both gene structure and amino acid sequence. These proteins are vital for maintaining water homeostasis in living organisms, especially for aquatic animals such as teleost fish. Studies on teleost Aqps are mainly limited to several model species with diploid genomes. Common carp, which has a tetraploidized genome, is one of the most common aquaculture species being adapted to a wide range of aquatic environments. The complete common carp genome has recently been released, providing us the possibility for gene evolution of aqp gene family after whole genome duplication.ResultsIn this study, we identified a total of 37 aqp genes from common carp genome. Phylogenetic analysis revealed that most of aqps are highly conserved. Comparative analysis was performed across five typical vertebrate genomes. We found that almost all of the aqp genes in common carp were duplicated in the evolution of the gene family. We postulated that the expansion of the aqp gene family in common carp was the result of an additional whole genome duplication event and that the aqp gene family in other teleosts has been lost in their evolution history with the reason that the functions of genes are redundant and conservation. Expression patterns were assessed in various tissues, including brain, heart, spleen, liver, intestine, gill, muscle, and skin, which demonstrated the comprehensive expression profiles of aqp genes in the tetraploidized genome. Significant gene expression divergences have been observed, revealing substantial expression divergences or functional divergences in those duplicated aqp genes post the latest WGD event.ConclusionsTo some extent, the gene families are also considered as a unique source for evolutionary studies. Moreover, the whole set of common carp aqp gene family provides an essential genomic resource for future biochemical, toxicological, physiological, and evolutionary studies in common carp.

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Section: Resultssupporting

confidence: 91%

Genome Wide Identification, Phylogeny, and Expression of Aquaporin Genes in Common Carp (Cyprinus carpio)

et al. 2016

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“…Our previous analyses of the evolution of piscine aquaporins provided evidence for four major grades of integral membrane proteins in Vertebrata [36], [42], [43]. More recently this concept has been extended to plants [77], [78], however the origin of plant glycerol transporters, including NIPs and GIPs, may have occurred via HGT [55], [56], indicating that the gene flows are not coalescent.…”

Section: Discussionmentioning

confidence: 99%

“…Consequently, both piscine and mammalian aquaporins can be phylogenetically and functionally classified as water-selective classical aquaporins (AQP0, -1, -2, -4, -5 and -6), an ammoniaporin (AQP8), which transports water, ammonia and urea, unorthodox aquaporins (AQP11, and -12) for which cell permation properties have yet to be identified, and classical aquaglyceroporins (Glp: AQP3, -7, -9 and -10), which facilitate the transport of water, arsenic, urea and polyols such as glycerol [36]–[41]. However, although the genomes of the five species of Teleostei studied were found to retain a larger repertoire of aquaporins due to an independent genomic duplication event at the root of the crown clade, they appeared to lack orthologs of AQP2, -5, or -6 [36], [42], [43]. By contrast, a study of lungfishes (Dipnoi) revealed that this ancient lineage of sarcopterygian fishes possess an AVT-AVPR2-AQP2-like system similar to Mammalia [44].…”

Section: Introductionmentioning

confidence: 99%

The Lineage-Specific Evolution of Aquaporin Gene Clusters Facilitated Tetrapod Terrestrial Adaptation

Finn

Chauvigné

Hlidberg³

et al. 2014

PLoS ONE

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A major physiological barrier for aquatic organisms adapting to terrestrial life is dessication in the aerial environment. This barrier was nevertheless overcome by the Devonian ancestors of extant Tetrapoda, but the origin of specific molecular mechanisms that solved this water problem remains largely unknown. Here we show that an ancient aquaporin gene cluster evolved specifically in the sarcopterygian lineage, and subsequently diverged into paralogous forms of AQP2, -5, or -6 to mediate water conservation in extant Tetrapoda. To determine the origin of these apomorphic genomic traits, we combined aquaporin sequencing from jawless and jawed vertebrates with broad taxon assembly of >2,000 transcripts amongst 131 deuterostome genomes and developed a model based upon Bayesian inference that traces their convergent roots to stem subfamilies in basal Metazoa and Prokaryota. This approach uncovered an unexpected diversity of aquaporins in every lineage investigated, and revealed that the vertebrate superfamily consists of 17 classes of aquaporins (Aqp0 - Aqp16). The oldest orthologs associated with water conservation in modern Tetrapoda are traced to a cluster of three aqp2-like genes in Actinistia that likely arose >500 Ma through duplication of an aqp0-like gene present in a jawless ancestor. In sea lamprey, we show that aqp0 first arose in a protocluster comprised of a novel aqp14 paralog and a fused aqp01 gene. To corroborate these findings, we conducted phylogenetic analyses of five syntenic nuclear receptor subfamilies, which, together with observations of extensive genome rearrangements, support the coincident loss of ancestral aqp2-like orthologs in Actinopterygii. We thus conclude that the divergence of sarcopterygian-specific aquaporin gene clusters was permissive for the evolution of water conservation mechanisms that facilitated tetrapod terrestrial adaptation.

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“…Compared to mammals, however, teleosts are known to harbor a larger repertoire of aquaporins due to the retention in the genome of two, or in some cases three, orthologs of the human counterparts [30,32,33]. Given that some teleost aquaporins, such as Aqp1ab expressed in the female germ line, are evolving more rapidly than the mammalian counterparts [34], it remains to be established whether the increased copy number of piscine aquaporins have evolved redundant or novel functions associated with the male reproductive biology of teleosts.…”

Section: Introductionmentioning

confidence: 99%

Subcellular Localization of Selectively Permeable Aquaporins in the Male Germ Line of a Marine Teleost Reveals Spatial Redistribution in Activated Spermatozoa1

Chauvigné

Boj

Vilella

et al. 2013

Biology of Reproduction

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In oviparous vertebrates such as the marine teleost gilthead seabream, water and fluid homeostasis associated with testicular physiology and the external activation of spermatozoa is potentially mediated by multiple aquaporins. To test this hypothesis, we isolated five novel members of the aquaporin superfamily from gilthead seabream and developed paralog-specific antibodies to localize the cellular sites of protein expression in the male reproductive tract. Together with phylogenetic classification, functional characterization of four of the newly isolated paralogs, Aqp0a, -7, -8b, and -9b, demonstrated that they were water permeable, while Aqp8b was also permeable to urea, and Aqp7 and -9b were permeable to glycerol and urea. Immunolocalization experiments indicated that up to seven paralogous aquaporins are differentially expressed in the seabream testis: Aqp0a and -9b in Sertoli and Leydig cells, respectively; Aqp1ab, -7, and -10b from spermatogonia to spermatozoa; and Aqp1aa and -8b in spermatids and sperm. In the efferent duct, only Aqp10b was found in the luminal epithelium. Ejaculated spermatozoa showed a segregated spatial distribution of five aquaporins: Aqp1aa and -7 in the entire flagellum or the head, respectively, and Aqp1ab, -8b, and -10b both in the head and the anterior tail. The combination of immunofluorescence microscopy and biochemical fractionation of spermatozoa indicated that Aqp10b and phosphorylated Aqp1ab are rapidly translocated to the head plasma membrane upon activation, whereas Aqp8b accumulates in the mitochondrion of the spermatozoa. In contrast, Aqp1aa and -7 remained unchanged. These data reveal that aquaporin expression in the teleost testis shares conserved features of the mammalian system, and they suggest that the piscine channels may play different roles in water and solute transport during spermatogenesis, sperm maturation and nutrition, and the initiation and maintenance of sperm motility.

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Aquaporin Evolution in Fishes

Cited by 55 publications

References 56 publications

Genome Wide Identification, Phylogeny, and Expression of Aquaporin Genes in Common Carp (Cyprinus carpio)

Genome Wide Identification, Phylogeny, and Expression of Aquaporin Genes in Common Carp (Cyprinus carpio)

The Lineage-Specific Evolution of Aquaporin Gene Clusters Facilitated Tetrapod Terrestrial Adaptation

Subcellular Localization of Selectively Permeable Aquaporins in the Male Germ Line of a Marine Teleost Reveals Spatial Redistribution in Activated Spermatozoa1

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