ArticleProceedings of the National Academy of Sciences of the United States of America2014
X-ray structure of human aquaporin 2 and its implications for nephrogenic diabetes insipidus and trafficking.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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66 citing papers in PubMed, 134 citations in OpenAlex.
- Structural and functional characterization of aquaporin 4 from the freshwater gastropod Pomacea canaliculata under temperature stress.Molecular biology reports · 2026Article
- Review
- Bridging structure and function: artificial intelligence-based modelling of kidney proteins.Nature reviews. Nephrology · 2026Review
- In Silico Modelling of the AQP0 T138R Mutation and its' links to Potential Mechanisms of Cataractogenesis.Research square · 2025Article
- Improved Pendant-Bearing Glucose-Neopentyl Glycols for Membrane Protein Stability.Bioconjugate chemistry · 2025Article
- Article
- Molecular mechanism of anion permeation through aquaporin 6.Biophysical journal · 2024Article
- Aquaporin Modulation by Cations, a Review.Current issues in molecular biology · 2024Review
- Structural Basis for the Interaction between the Ezrin FERM-Domain and Human Aquaporins.International journal of molecular sciences · 2024Article
- Aquaporins in colorectal cancer: exploring their role in tumorigenesis, metastasis, and drug response.Human cell · 2024Review
- Deciphering Molecular Mechanisms Involved in the Modulation of Human Aquaporins' Water Permeability by Zinc Cations: A Molecular Dynamics Approach.International journal of molecular sciences · 2024Article
- Molecular basis for human aquaporin inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural and functional analysis of aquaporin-2 mutants involved in nephrogenic diabetes insipidus.Scientific reports · 2023Article
- Cryo-EM structure supports a role of AQP7 as a junction protein.Nature communications · 2023Article
- Protein Structure and Modification of Aquaporins.Advances in experimental medicine and biology · 2023Article
- Exploring the diversity of AVPR2 in Primates and its evolutionary implications.Genetics and molecular biology · 2023Article
- Does the composition of urinary extracellular vesicles reflect the abundance of renal NaPflugers Archiv : European journal of physiology · 2022Article
- Yeast as a tool for membrane protein production and structure determination.FEMS yeast research · 2022Article
- Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels.International journal of molecular sciences · 2022Review
- High-yield overproduction and purification of human aquaporins fromSTAR protocols · 2022Article
6 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human aquaporin 2 (AQP2) is a water channel found in the kidney collecting duct, where it plays a key role in concentrating urine. Water reabsorption is regulated by AQP2 trafficking between intracellular storage vesicles and the apical membrane. This process is tightly controlled by the pituitary hormone arginine vasopressin and defective trafficking results in nephrogenic diabetes insipidus (NDI). Here we present the X-ray structure of human AQP2 at 2.75 Å resolution. The C terminus of AQP2 displays multiple conformations with the C-terminal α-helix of one protomer interacting with the cytoplasmic surface of a symmetry-related AQP2 molecule, suggesting potential protein-protein interactions involved in cellular sorting of AQP2. Two Cd(2+)-ion binding sites are observed within the AQP2 tetramer, inducing a rearrangement of loop D, which facilitates this interaction. The locations of several NDI-causing mutations can be observed in the AQP2 structure, primarily situated within transmembrane domains and the majority of which cause misfolding and ER retention. These observations provide a framework for understanding why mutations in AQP2 cause NDI as well as structural insights into AQP2 interactions that may govern its trafficking.
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