ArticleThe Journal of biological chemistry2008
Phosphorylation determines the calmodulin-mediated Ca2+ response and water permeability of AQP0.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 38 citations in OpenAlex.
- Characterization of human aquaporin ion channels in a yeast expression system as a tool for novel ion channel discovery.Bioscience reports · 2024Article
- The role of phosphorylation in calmodulin-mediated gating of human AQP0.The Biochemical journal · 2024Article
- Modulation of Membrane Trafficking of AQP5 in the Lens in Response to Changes in Zonular Tension Is Mediated by the Mechanosensitive Channel TRPV1.International journal of molecular sciences · 2023Article
- Protein Structure and Modification of Aquaporins.Advances in experimental medicine and biology · 2023Article
- Molecular mechanisms governing aquaporin relocalisation.Biochimica et biophysica acta. Biomembranes · 2022Review
- The relationship between major intrinsic protein genes and cataract.International ophthalmology · 2021Review
- Dynamics of Salivary Gland AQP5 under Normal and Pathologic Conditions.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
- Review
- Aqp0a Regulates Suture Stability in the Zebrafish Lens.Investigative ophthalmology & visual science · 2018Article
- Role of Pore-Lining Residues in Defining the Rate of Water Conduction by Aquaporin-0.Biophysical journal · 2017Article
- Calmodulin Gates Aquaporin 0 Permeability through a Positively Charged Cytoplasmic Loop.The Journal of biological chemistry · 2017Article
- Spatial distributions of phosphorylated membrane proteins aquaporin 0 and MP20 across young and aged human lenses.Experimental eye research · 2016Article
- Identification and Molecular Mechanisms of the Rapid Tonicity-induced Relocalization of the Aquaporin 4 Channel.The Journal of biological chemistry · 2015Article
- Intact and N- or C-terminal end truncated AQP0 function as open water channels and cell-to-cell adhesion proteins: end truncation could be a prelude for adjusting the refractive index of the lens to prevent spherical aberration.Biochimica et biophysica acta · 2014Article
- The aquaporin zero puzzle.Biophysical journal · 2014Review
- Aquaporins in the eye: expression, function, and roles in ocular disease.Biochimica et biophysica acta · 2014Review
- In vivo analysis of aquaporin 0 function in zebrafish: permeability regulation is required for lens transparency.Investigative ophthalmology & visual science · 2013Article
- Mass spectrometry of membrane proteins: a focus on aquaporins.Biochemistry · 2013Review
- Regulation of AQP0 water permeability is enhanced by cooperativity.The Journal of general physiology · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In Xenopus oocytes, the water permeability of AQP0 (P(f)) increases with removal of external calcium, an effect that is mediated by cytoplasmic calmodulin (CaM) bound to the C terminus of AQP0. To investigate the effects of serine phosphorylation on CaM-mediated Ca(2+) regulation of P(f), we tested the effects of kinase activation, CaM inhibition, and a series of mutations in the C terminus CaM binding site. Calcium regulation of AQP0 P(f) manifests four distinct phenotypes: Group 1, with high P(f) upon removal of external Ca(2+) (wild-type, S229N, R233A, S235A, S235K, K238A, and R241E); Group 2, with high P(f) in elevated (5 mm) external Ca(2+) (S235D and R241A); Group 3, with high P(f) and no Ca(2+) regulation (S229D, S231N, S231D, S235N, and S235N/I236S); and Group 4, with low P(f) and no Ca(2+) regulation (protein kinase A and protein kinase C activators, S229D/S235D and S235N/I236S). Within each group, we tested whether CaM binding mediates the phenotype, as shown previously for wild-type AQP0. In the presence of calmidazolium, a CaM inhibitor, S235D showed high P(f) and no Ca(2+) regulation, suggesting that S235D still binds CaM. Contrarily, S229D showed a decrease in recruitment of CaM, suggesting that S229D is unable to bind CaM. Taken together, our results suggest a model in which CaM acts as an inhibitor of AQP0 P(f). CaM binding is associated with a low P(f) state, and a lack of CaM binding is associated with a high P(f) state. Pathological conditions of inappropriate phosphorylation or calcium/CaM regulation could induce P(f) changes contributing to the development of a cataract.
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