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Cells
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Perspectives on the Evolution of Aquaporin Superfamily
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Perspectives on the Evolution of Aquaporin Superfamily

A special issue of Cells (ISSN 2073-4409).

Deadline for manuscript submissions: closed (31 October 2021) | Viewed by 8904

Special Issue Editor

Prof. Kenichi Ishibashi

E-Mail Website
Guest Editor
Department of Medical Physiology, School of Pharmacy, Meiji Pharmaceutical University, 2-522-1 Noshio, Kiyose, Tokyo 204–8588, Japan
Interests: transporter; channel; electrolyte homeostasis; nephrology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Aquaporin (AQP) belongs to an ancient channel family with a highly conserved structure stemming from bacteria. Genome projects have accumulated many AQP-like sequences containing a conserved signature sequence for an AQP superfamily and a pair of NPA (Asn-Pro-Ala) boxes, even with an overall homology of less than 30%. The analysis of their primary sequences is instrumental to speculate their function and adaptive roles in altered environments. Moreover, evolutional viewpoints of AQPs will shed light on the distribution and regulation of AQPs. Accordingly, we are excited to recruit a repertoire of AQPs from a variety of organisms, which is expected to expand the AQP research field. We welcome manuscripts of any kind on aspects of evolution and regulation of AQPs from this perspective.

Prof. Kenichi Ishibashi
Guest Editor

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Keywords

  • aquaporin
  • evolution
  • genomics
  • classification
  • distribution
  • regulation
  • function

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Published Papers (3 papers)

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Research

17 pages, 3463 KiB  
Article
Finding Aquaporins in Annelids: An Evolutionary Analysis and a Case Study
by Serena Mucciolo, Andrea Desiderato, Marika Salonna, Tomasz Mamos, Viviane Prodocimo, Maikon Di Domenico, Francesco Mastrototaro, Paulo Lana, Carmela Gissi and Giuseppe Calamita
Cells 2021, 10(12), 3562; https://doi.org/10.3390/cells10123562 - 17 Dec 2021
Cited by 2 | Viewed by 3186
Abstract
Aquaporins (AQPs) are a family of membrane channels facilitating diffusion of water and small solutes into and out of cells. Despite their biological relevance in osmoregulation and ubiquitous distribution throughout metazoans, the presence of AQPs in annelids has been poorly investigated. Here, we [...] Read more.
Aquaporins (AQPs) are a family of membrane channels facilitating diffusion of water and small solutes into and out of cells. Despite their biological relevance in osmoregulation and ubiquitous distribution throughout metazoans, the presence of AQPs in annelids has been poorly investigated. Here, we searched and annotated Aqp sequences in public genomes and transcriptomes of annelids, inferred their evolutionary relationships through phylogenetic analyses and discussed their putative physiological relevance. We identified a total of 401 Aqp sequences in 27 annelid species, including 367 sequences previously unrecognized as Aqps. Similar to vertebrates, phylogenetic tree reconstructions clustered these annelid Aqps in four clades: AQP1-like, AQP3-like, AQP8-like and AQP11-like. We found no clear indication of the existence of paralogs exclusive to annelids; however, several gene duplications seem to have occurred in the ancestors of some Sedentaria annelid families, mainly in the AQP1-like clade. Three of the six Aqps annotated in Alitta succinea, an estuarine annelid showing high salinity tolerance, were validated by RT-PCR sequencing, and their similarity to human AQPs was investigated at the level of “key” conserved residues and predicted three-dimensional structure. Our results suggest a diversification of the structures and functions of AQPs in Annelida comparable to that observed in other taxa. Full article
(This article belongs to the Special Issue Perspectives on the Evolution of Aquaporin Superfamily)
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13 pages, 2665 KiB  
Communication
First Glimpse at the Diverse Aquaporins of Amphipod Crustaceans
by Andrea Desiderato, Tomasz Mamos, Tomasz Rewicz, Artur Burzynski and Serena Mucciolo
Cells 2021, 10(12), 3417; https://doi.org/10.3390/cells10123417 - 4 Dec 2021
Cited by 2 | Viewed by 2480
Abstract
The importance of aquaporins (AQPs) in the transport of water and solutes through cell membranes is well recognized despite being relatively new. To date, despite their abundance, diversity, and presence in disparate environments, amphipods have only been mentioned in studies about the AQPs [...] Read more.
The importance of aquaporins (AQPs) in the transport of water and solutes through cell membranes is well recognized despite being relatively new. To date, despite their abundance, diversity, and presence in disparate environments, amphipods have only been mentioned in studies about the AQPs of other animals and have never been further investigated. In this work, we aimed to recover from public data available AQPs of these crustaceans and reconstruct phylogenetic affinities. We first performed BLAST searches with several queries of diverse taxa against different NCBI databases. Then, we selected the clades of AQPs retrieving the amphipod superfamily Gammaroidea as monophyletic and ran phylogenetic analyses to assess their performances. Our results show how most of the AQPs of amphipods are similar to those of other crustaceans, despite the Prip-like displayed different paralogs, and report for the first time a putative Aqp8-like for arthropods. We also found that the candidate genes of Prip-like, Bib-like, Aqp12-like, and Glp-like help solve deeper relationships in phylogenies of amphipods while leaving uncertainties in shallower parts. With our findings, we hope to increase attention to the study of amphipods as models for AQP functioning and evolution. Full article
(This article belongs to the Special Issue Perspectives on the Evolution of Aquaporin Superfamily)
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Graphical abstract

9 pages, 1292 KiB  
Article
Differences in a Single Extracellular Residue Underlie Adhesive Functions of Two Zebrafish Aqp0s
by Irene Vorontsova, James E. Hall, Thomas F. Schilling, Noriaki Nagai and Yosuke Nakazawa
Cells 2021, 10(8), 2005; https://doi.org/10.3390/cells10082005 - 6 Aug 2021
Cited by 3 | Viewed by 2368
Abstract
Aquaporin 0 (AQP0) is the most abundant lens membrane protein, and loss of function in human and animal models leads to cataract formation. AQP0 has several functions in the lens including water transport and adhesion. Since lens optics rely on strict tissue architecture [...] Read more.
Aquaporin 0 (AQP0) is the most abundant lens membrane protein, and loss of function in human and animal models leads to cataract formation. AQP0 has several functions in the lens including water transport and adhesion. Since lens optics rely on strict tissue architecture achieved by compact cell-to-cell adhesion between lens fiber cells, understanding how AQP0 contributes to adhesion would shed light on normal lens physiology and pathophysiology. We show in an in vitro adhesion assay that one of two closely related zebrafish Aqp0s, Aqp0b, has strong auto-adhesive properties while Aqp0a does not. The difference appears to be largely due to a single amino acid difference at residue 110 in the extracellular C-loop, which is T in Aqp0a and N in Aqp0b. Similarly, P110 is the key residue required for adhesion in mammalian AQP0, highlighting the importance of residue 110 in AQP0 cell-to-cell adhesion in vertebrate lenses as well as the divergence of adhesive and water permeability functions in zebrafish duplicates. Full article
(This article belongs to the Special Issue Perspectives on the Evolution of Aquaporin Superfamily)
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