Article (Scientific journals)
The zebrafish genome encodes the largest vertebrate repertoire of functional aquaporins with dual paralogy and substrate specificities similar to mammals
Tingaud-Sequeira, Angèle; Calusinska, Magdalena; Finn, Roderick N et al.
2010In BMC Evolutionary Biology, 10
Peer Reviewed verified by ORBi
 

Files


Full Text
Zebrafish aquaporins 2010.pdf
Publisher postprint (3.61 MB)
Request a copy

All documents in ORBi are protected by a user license.

Send to



Details



Keywords :
zebrafish; aquaporins
Abstract :
[en] Background: Aquaporins are integral membrane proteins that facilitate the transport of water and small solutes across cell membranes. These proteins are vital for maintaining water homeostasis in living organisms. In mammals, thirteen aquaporins (AQP0-12) have been characterized, but in lower vertebrates, such as fish, the diversity, structure and substrate specificity of these membrane channel proteins are largely unknown. Results: The screening and isolation of transcripts from the zebrafish (Danio rerio) genome revealed eighteen sequences structurally related to the four subfamilies of tetrapod aquaporins, i.e., aquaporins (AQP0, -1 and -4), water and glycerol transporters or aquaglyceroporins (Glps; AQP3 and AQP7-10), a water and urea transporter (AQP8), and two unorthodox aquaporins (AQP11 and -12). Phylogenetic analyses of nucleotide and deduced amino acid sequences demonstrated dual paralogy between teleost and human aquaporins. Three of the duplicated zebrafish isoforms have unlinked loci, two have linked loci, while DrAqp8 was found in triplicate across two chromosomes. Genomic sequencing, structural analysis, and maximum likelihood reconstruction, further revealed the presence of a putative pseudogene that displays hybrid exons similar to tetrapod AQP5 and -1. Ectopic expression of the cloned transcripts in Xenopus laevis oocytes demonstrated that zebrafish aquaporins and Glps transport water or water, glycerol and urea, respectively, whereas DrAqp11b and -12 were not functional in oocytes. Contrary to humans and some rodents, intrachromosomal duplicates of zebrafish AQP8 were water and urea permeable, while the genomic duplicate only transported water. All aquaporin transcripts were expressed in adult tissues and found to have divergent expression patterns. In some tissues, however, redundant expression of transcripts encoding two duplicated paralogs seems to occur. Conclusion: The zebrafish genome encodes the largest repertoire of functional vertebrate aquaporins with dual paralogy to human isoforms. Our data reveal an early and specific diversification of these integral membrane proteins at the root of the crown-clade of Teleostei. Despite the increase in gene copy number, zebrafish aquaporins mostly retain the substrate specificity characteristic of the tetrapod counterparts. Based upon the integration of phylogenetic, genomic and functional data we propose a new classification for the piscine aquaporin superfamily.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Tingaud-Sequeira, Angèle
Calusinska, Magdalena ;  Université de Liège - ULiège > Centre d'ingénierie des protéines
Finn, Roderick N
Chauvigné, François
Lozano
Cerdà, Joan
Language :
English
Title :
The zebrafish genome encodes the largest vertebrate repertoire of functional aquaporins with dual paralogy and substrate specificities similar to mammals
Alternative titles :
[en] The zebrafish genome encodes the largest vertebrate repertoire of functional aquaporins with dual paralogy and substrate specificities similar to mammals
Publication date :
2010
Journal title :
BMC Evolutionary Biology
eISSN :
1471-2148
Publisher :
BioMed Central
Volume :
10
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 24 January 2012

Statistics


Number of views
62 (1 by ULiège)
Number of downloads
0 (0 by ULiège)

Scopus citations®
 
143
Scopus citations®
without self-citations
114
OpenCitations
 
127

Bibliography


Similar publications



Contact ORBi