Evolutionary Overview of Aquaporin Superfamily

Ishibashi, Keiichiro; Tanaka, Yasuko; Morishita, Yoshiyuki

doi:10.1007/978-981-19-7415-1_6

Cited by 5 publications

(1 citation statement)

References 98 publications

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“…AQPs are ancient and present in all kingdoms of life [ 4 ]. They share a common protein fold consisting of six transmembrane spans and two so-called half-helices that meet in the center of the lipid bilayer to form a pseudo-seventh transmembrane domain [ 5 ].…”

Section: Introductionmentioning

confidence: 99%

Methylthiosulfonate-Based Cysteine Modifiers as Alternative Inhibitors of Mercurial-Sensitive Aquaporins

Jeuken,

Jaeger,

Matthews

et al. 2023

Cells

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(1) Background: Several members of the ubiquitous aquaporin family, AQP, of water and neutral solute channels carry a cysteine residue in the selectivity filter region. Traditionally, toxic mercury-containing compounds are used to bind to the cysteine as covalent AQP inhibitors for physiological studies or analysis of structure–function relationships. (2) Methods: We tested thiol-reactive methylthiosulfonate reagents, MTS, as alternative Cys modifiers for AQP inhibition. Three MTS reagents transferring S-alkyl moieties of increasing size, i.e., S-methyl, S-n-propyl, and S-benzyl, were used with yeast-expressed water-selective AQP1 and the aquaglyceroporin AQP9. Respective Cys-to-Ala variants and mouse erythrocytes that naturally express AQP1 and AQP9 served as controls. (3) Results: Both wildtype AQP isoforms were inhibited by the Cys modifiers in a size-dependent manner, whereas the Cys-to-Ala-variants exhibited resistance. Sub-millimolar concentrations and incubation times in the minute range were sufficient. The modifications were reversible by treatment with the thiol reagents acetylcysteine, ACC, and dithiothreitol, DTT. (4) Conclusions: MTS reagents represent a valid alternative of low toxicity for the inhibition of mercurial-sensitive AQPs.

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Section: Introductionmentioning

confidence: 99%

Methylthiosulfonate-Based Cysteine Modifiers as Alternative Inhibitors of Mercurial-Sensitive Aquaporins

Jeuken,

Jaeger,

Matthews

et al. 2023

Cells

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Early Diversification of Membrane Intrinsic Proteins (MIPs) in Eukaryotes

Irisarri,

Lorente-Martínez,

Strassert

et al. 2024

Genome Biology and Evolution

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Membrane intrinsic proteins (MIPs), including aquaporins (AQPs) and aquaglyceroporins (GLPs), form an ancient family of transporters for water and small solutes across biological membranes. The evolutionary history and functions of MIPs have been extensively studied in vertebrates and land plants, but their widespread presence across the eukaryotic tree of life suggests both a more complex evolutionary history and a broader set of functions than previously thought. That said, the early evolution of MIPs remains obscure. The presence of four AQP and one GLP clades across both Bacteria and Archaea suggests that the first eukaryotes could have possessed up to five MIPs. Here, we report on a previously unknown richness in MIP diversity across all major eukaryotic lineages, including unicellular eukaryotes, which make up the bulk of eukaryotic diversity. Three MIP clades have likely deep evolutionary origins, dating back to the last eukaryotic common ancestor (LECA), and support the presence of a complex MIP repertoire in early eukaryotes. Overall, our findings highlight the growing complexity of the reconstructed LECA genome: the dynamic evolutionary history of MIPs was set in motion when eukaryotes were in their infancy followed by radiative bursts across all main eukaryotic lineages.

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Chromosome‐level genome of diamondback terrapin provides insight into the genetic basis of salinity adaptation

JIANG,

WANG,

ZHAI

et al. 2024

Integr. Zool.

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Diamondback terrapins (Malaclemys terrapin centrata) exhibit strong environmental adaptability and live in both freshwater and saltwater. However, the genetic basis of this adaptability has not been the focus of research. In this study, we successfully constructed a ∼2.21‐Gb chromosome‐level genome assembly for M. t. centrata using high‐coverage and high‐depth genomic sequencing data generated on multiple platforms. The M. t. centrata genome contains 25 chromosomes and the scaffold N50 of ∼143.75 Mb, demonstrating high continuity and accuracy. In total, 53.82% of the genome assembly was composed of repetitive sequences, and 22 435 protein‐coding genes were predicted. Our phylogenetic analysis indicated that M. t. centrata was closely related to the red‐eared slider turtle (Trachemys scripta elegans), with divergence approximately ∼23.6 million years ago (Mya) during the early Neogene period of the Cenozoic era. The population size of M. t. centrata decreased significantly over the past ∼14 Mya during the Cenozoic era. Comparative genomic analysis indicated that 36 gene families related to ion transport were expanded and several genes (AQP3, solute carrier subfamily, and potassium channel genes) underwent specific amino acid site mutations in the M. t. centrata genome. Changes to these ion transport‐related genes may have contributed to the remarkable salinity adaptability of diamondback terrapin. The results of this study not only provide a high‐quality reference genome for M. t. centrata but also elucidate the possible genetic basis for salinity adaptation in this species.

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Evolutionary Overview of Aquaporin Superfamily

Cited by 5 publications

References 98 publications

Methylthiosulfonate-Based Cysteine Modifiers as Alternative Inhibitors of Mercurial-Sensitive Aquaporins

Methylthiosulfonate-Based Cysteine Modifiers as Alternative Inhibitors of Mercurial-Sensitive Aquaporins

Early Diversification of Membrane Intrinsic Proteins (MIPs) in Eukaryotes

Chromosome‐level genome of diamondback terrapin provides insight into the genetic basis of salinity adaptation

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