ArticleScientific reports2016
Functional Recovery of AQP2 Recessive Mutations Through Hetero-Oligomerization with Wild-Type Counterpart.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Genetic analysis of nephrogenic diabetes insipidus patients: A study on the Iranian population.Molecular genetics & genomic medicine · 2024Article
- Further evidence for functional recovery of AQP2 mutations associated with nephrogenic diabetes insipidus.Physiological reports · 2021Article
- FungalBiomolecules · 2021Article
- NovelFrontiers in endocrinology · 2021Article
- Molecular Characterization of an Aquaporin-2 Mutation Causing Nephrogenic Diabetes Insipidus.Frontiers in endocrinology · 2021Article
- Molecular characterization of an aquaporin-2 mutation causing a severe form of nephrogenic diabetes insipidus.Cellular and molecular life sciences : CMLS · 2020Article
- Plant and Mammal Aquaporins: Same but Different.International journal of molecular sciences · 2018Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporin-2 (AQP2) is a homotetrameric water channel responsible for the final water reuptake in the kidney. Mutations in the protein induce nephrogenic diabetes insipidus (NDI), which challenges the water balance by producing large urinary volumes. Although recessive AQP2 mutations are believed to generate non-functional and monomeric proteins, the literature identifies several mild mutations which suggest the existence of mixed wt/mut tetramers likely to carry function in heterozygotes. Using Xenopus oocytes, we tested this hypothesis and found that mild mutants (V24A, D150E) can associate with wt-AQP2 in mixed heteromers, providing clear functional gain in the process (62 ± 17% and 63 ± 17% increases, respectively), conversely to the strong monomeric R187C mutant which fails to associate with wt-AQP2. In kidney cells, both V24A and D150E display restored targeting while R187C remains in intracellular stores. Using a collection of mutations to expand recovery analyses, we demonstrate that inter-unit contacts are central to this recovery process. These results not only present the ground data for the functional recovery of recessive AQP2 mutants through heteromerization, which prompt to revisit the accepted NDI model, but more importantly describe a general recovery process that could impact on all multimeric systems where recessive mutations are found.
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