ArticleStructure (London, England : 1993)2008
Noncanonical binding of calmodulin to aquaporin-0: implications for channel regulation.
Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
54 citing papers in PubMed, 75 citations in OpenAlex.
- Calcium induced N-terminal gating and pore collapse in connexin-46/50 gap junctions.Nature communications · 2026Article
- Preventing Age-Related Nuclear Cataract Development - Is Cholesterol the Key?Investigative ophthalmology & visual science · 2026Review
- Evaluating protein complexes between human aquaporin and calmodulin using biomolecular fluorescence complementation.Scientific reports · 2025Article
- Calcium induced N-terminal gating and pore collapse in connexin-46/50 gap junctions.bioRxiv : the preprint server for biology · 2025Article
- Aquaporin Modulation by Cations, a Review.Current issues in molecular biology · 2024Review
- The role of phosphorylation in calmodulin-mediated gating of human AQP0.The Biochemical journal · 2024Article
- Aquaporin water channels: roles beyond renal water handling.Nature reviews. Nephrology · 2023Review
- Protein Structure and Modification of Aquaporins.Advances in experimental medicine and biology · 2023Article
- Insight into the Mammalian Aquaporin Interactome.International journal of molecular sciences · 2022Review
- Molecular mechanisms governing aquaporin relocalisation.Biochimica et biophysica acta. Biomembranes · 2022Review
- Lens Aquaporins in Health and Disease: Location is Everything!Frontiers in physiology · 2022Review
- Calmodulin-Connexin Partnership in Gap Junction Channel Regulation-Calmodulin-Cork Gating Model.International journal of molecular sciences · 2021Review
- Regulation of Connexin Gap Junctions and Hemichannels by Calcium and Calcium Binding Protein Calmodulin.International journal of molecular sciences · 2020Review
- Connexin-46/50 in a dynamic lipid environment resolved by CryoEM at 1.9 Å.Nature communications · 2020Article
- Article
- Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.Progress in retinal and eye research · 2020Review
- Calmodulin-Mediated Regulation of Gap Junction Channels.International journal of molecular sciences · 2020Review
- BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability.Experimental eye research · 2019Article
- Cooperativity and allostery in aquaporin 0 regulation by CaBiochimica et biophysica acta. Biomembranes · 2019Article
- Covalently Linking Oligomerization-Impaired GlpF Protomers Does Not Completely Re-establish Wild-Type Channel Activity.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Aquaporins (AQPs) are a family of ubiquitous membrane channels that conduct water across cell membranes. AQPs form homotetramers containing four functional and independent water pores. Aquaporin-0 (AQP0) is expressed in the eye lens, where its water permeability is regulated by calmodulin (CaM). Here we use a combination of biochemical methods and NMR spectroscopy to probe the interaction between AQP0 and CaM. We show that CaM binds the AQP0 C-terminal domain in a calcium-dependent manner. We demonstrate that only two CaM molecules bind a single AQP0 tetramer in a noncanonical fashion, suggesting a form of cooperativity between AQP0 monomers. Based on these results, we derive a structural model of the AQP0/CaM complex, which suggests CaM may be inhibitory to channel permeability by capping the vestibules of two monomers within the AQP0 tetramer. Finally, phosphorylation within AQP0's CaM binding domain inhibits the AQP0/CaM interaction, suggesting a temporal regulatory mechanism for complex formation.
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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.