ArticleNature structural & molecular biology2013
Allosteric mechanism of water-channel gating by Ca2+-calmodulin.
Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
What it found
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Who cites it
70 citing papers in PubMed, 111 citations in OpenAlex.
- Calcium induced N-terminal gating and pore collapse in connexin-46/50 gap junctions.Nature communications · 2026Article
- Piezo1-mediated mechanohydraulic control of cell volume drives cardiac morphogenesis.Science advances · 2026Article
- Atomistic Insights into Anomeric and Stereochemical Effects on Glucose Transport by GLUTs.Journal of the American Chemical Society · 2026Article
- Evaluating protein complexes between human aquaporin and calmodulin using biomolecular fluorescence complementation.Scientific reports · 2025Article
- Lysine acetylation of aquaporin-3 promotes water permeability but is not essential for urine concentrating ability.American journal of physiology. Renal physiology · 2025Article
- Calcium induced N-terminal gating and pore collapse in connexin-46/50 gap junctions.bioRxiv : the preprint server for biology · 2025Article
- Oxidative stress-related genes in uveal melanoma: the role of CALM1 in modulating oxidative stress and apoptosis and its prognostic significance.Frontiers in oncology · 2025Article
- Aquaporin-0-protein interactions elucidated by crosslinking mass spectrometry.Biochemical and biophysical research communications · 2024Article
- Zebrafish Optical Development Requires Regulated Water Permeability by Aquaporin 0.Investigative ophthalmology & visual science · 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
- 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
- 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
- Endothelial Dysfunction in Neurodegenerative Diseases.International journal of molecular sciences · 2023Review
- Cortisol Interaction with Aquaporin-2 Modulates Its Water Permeability: Perspectives for Non-Genomic Effects of Corticosteroids.International journal of molecular sciences · 2023Article
- Classification and Gene Structure of Aquaporins.Advances in experimental medicine and biology · 2023Article
- Protein Structure and Modification of Aquaporins.Advances in experimental medicine and biology · 2023Article
- Expression Regulation and Trafficking of Aquaporins.Advances in experimental medicine and biology · 2023Review
- Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels.International journal of molecular sciences · 2022Review
10 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Calmodulin (CaM) is a universal regulatory protein that communicates the presence of calcium to its molecular targets and correspondingly modulates their function. This key signaling protein is important for controlling the activity of hundreds of membrane channels and transporters. However, understanding of the structural mechanisms driving CaM regulation of full-length membrane proteins has remained elusive. In this study, we determined the pseudoatomic structure of full-length mammalian aquaporin-0 (AQP0, Bos taurus) in complex with CaM, using EM to elucidate how this signaling protein modulates water-channel function. Molecular dynamics and functional mutation studies reveal how CaM binding inhibits AQP0 water permeability by allosterically closing the cytoplasmic gate of AQP0. Our mechanistic model provides new insight, only possible in the context of the fully assembled channel, into how CaM regulates multimeric channels by facilitating cooperativity between adjacent subunits.
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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.