ArticleFEBS open bio2014
The role of Cysteine 227 in subcellular localization, water permeability, and multimerization of aquaporin-11.
Article in FEBS open bio, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Cryo-EM structure of human AQP11 reveals a trimeric architecture with a large pore.Science advances · 2026Article
- Classification and Gene Structure of Aquaporins.Advances in experimental medicine and biology · 2023Article
- Aquaporins in Immune Cells and Inflammation: New Targets for Drug Development.International journal of molecular sciences · 2021Review
- Involvement of the NADPH oxidase 2 pathway in renal oxidative stress inBiochemistry and biophysics reports · 2019Article
- Cooperativity in Plant Plasma Membrane Intrinsic Proteins (PIPs): Mechanism of Increased Water Transport in Maize PIP1 Channels in Hetero-tetramers.Scientific reports · 2018Article
- Expression and Distribution Pattern of Aquaporin 4, 5 and 11 in Retinas of 15 Different Species.International journal of molecular sciences · 2016Article
- Astrocyte Aquaporin Dynamics in Health and Disease.International journal of molecular sciences · 2016Review
- Aquaporin 11, a regulator of water efflux at retinal Müller glial cell surface decreases concomitant with immune-mediated gliosis.Journal of neuroinflammation · 2016Article
- Temporal Aquaporin 11 Expression and Localization during Preimplantation Embryo Development.Development & reproduction · 2015Article
- Genetic predisposition of donors affects the allograft outcome in kidney transplantation: Single-nucleotide polymorphism of aquaporin-11.Kidney research and clinical practice · 2015Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporin-11 (AQP11) is the latest member of the mammalian water channel protein family to be described. Recent in vivo studies have shown that mutation at Cys(227) causes renal failure. However the importance of Cys(227) for the molecular function of AQP11 is largely unknown. In this study, we examined the subcellular localization, water permeability, and multimerization of AQP11 with a mutation at Cys(227). Interestingly, cells expressing the mutants had significantly higher osmotic water permeability. In contrast, the mutation lowered the cell surface expression and multimerization levels. Our observations suggest that Cys(227) is crucial for the proper molecular function of AQP11.
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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.