ArticleProceedings of the National Academy of Sciences of the United States of America2008
High-resolution x-ray structure of human aquaporin 5.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.
What it found
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Who cites it
120 citing papers in PubMed, 215 citations in OpenAlex.
- Cryo-EM structure of human AQP11 reveals a trimeric architecture with a large pore.Science advances · 2026Article
- The role of NEDD4-mediated ubiquitination of AQP5 in allergic rhinitis: implications for nasal mucosal barrier function.Frontiers in immunology · 2026Article
- Simulating Gas Permeation Through the Central Pore of AQP5.Advances in experimental medicine and biology · 2026Article
- Structural insights into AQP3 channel closure upon pH and redox changes reveal an autoregulatory molecular mechanism.Nature communications · 2025Article
- CLIP2: a novel functional player in AQP5 trafficking dynamics and implications for Sjögren's disease.Cell communication and signaling : CCS · 2025Article
- Aquaporins: a novel perspective in the treatment of lung diseases.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2025Review
- Aquaporins in lipid metabolism: functions and regulation in health and disease.Lipids in health and disease · 2025Review
- AQP5 trafficking is regulated by its C-terminal tail and interaction with prolactin-inducible protein.Biology direct · 2025Article
- Article
- Quaternary arrangements of membrane proteins: an aquaporin case.Biochemical Society transactions · 2024Review
- Dimerization is required for the glycosylation of S1-S2 linker of sea urchin voltage-gated proton channel Hv1.Biophysical journal · 2024Article
- Molecular mechanism of anion permeation through aquaporin 6.Biophysical journal · 2024Article
- Structural Basis for the Interaction between the Ezrin FERM-Domain and Human Aquaporins.International journal of molecular sciences · 2024Article
- Efficient generation of a stable CHO-K1 cell line overexpressing the human water channel aquaporin-5 as tool to generate therapeutic antibodies.Scientific reports · 2024Article
- Aquaporins in colorectal cancer: exploring their role in tumorigenesis, metastasis, and drug response.Human cell · 2024Review
- Peroxiporins in Triple-Negative Breast Cancer: Biomarker Potential and Therapeutic Perspectives.International journal of molecular sciences · 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
- The involvement of aquaporin 5 in the inflammatory response of primary Sjogren's syndrome dry eye: potential therapeutic targets exploration.Frontiers in medicine · 2024Review
- Small-angle scattering from flat bilayers containing correlated scattering length density inhomogeneities.Journal of applied crystallography · 2023Article
60 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human aquaporin 5 (HsAQP5) facilitates the transport of water across plasma membranes and has been identified within cells of the stomach, duodenum, pancreas, airways, lungs, salivary glands, sweat glands, eyes, lacrimal glands, and the inner ear. AQP5, like AQP2, is subject to posttranslational regulation by phosphorylation, at which point it is trafficked between intracellular storage compartments and the plasma membrane. Details concerning the molecular mechanism of membrane trafficking are unknown. Here we report the x-ray structure of HsAQP5 to 2.0-A resolution and highlight structural similarities and differences relative to other eukaryotic aquaporins. A lipid occludes the putative central pore, preventing the passage of gas or ions through the center of the tetramer. Multiple consensus phosphorylation sites are observed in the structure and their potential regulatory role is discussed. We postulate that a change in the conformation of the C terminus may arise from the phosphorylation of AQP5 and thereby signal trafficking.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.