ArticleInvestigative ophthalmology & visual science2011
Aquaporin-0 interacts with the FERM domain of ezrin/radixin/moesin proteins in the ocular lens.
Article in Investigative ophthalmology & visual science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 45 citations in OpenAlex.
- Loss of cyclase-associated protein 2 alters actin cytoskeleton organization and biomechanical properties of the ocular lens.Journal of cell science · 2026Article
- Cyclase associated actin cytoskeleton regulatory protein 2 (CAP2) organizes the actin cytoskeleton to influence the biomechanical properties of the ocular lens.bioRxiv : the preprint server for biology · 2025Article
- Aquaporin-0-protein interactions elucidated by crosslinking mass spectrometry.Biochemical and biophysical research communications · 2024Article
- Molecular Dynamics Simulations of the Eye Lens Water Channel Aquaporin 0 from Fish.The journal of physical chemistry. B · 2024Article
- Structural Basis for the Interaction between the Ezrin FERM-Domain and Human Aquaporins.International journal of molecular sciences · 2024Article
- Regulation of water flow in the ocular lens: new roles for aquaporins.The Journal of physiology · 2024Review
- Aquaporin water channels: roles beyond renal water handling.Nature reviews. Nephrology · 2023Review
- Methods for studying mammalian aquaporin biology.Biology methods & protocols · 2023Review
- Insight into the Mammalian Aquaporin Interactome.International journal of molecular sciences · 2022Review
- Lens Aquaporins in Health and Disease: Location is Everything!Frontiers in physiology · 2022Review
- Spatially Resolved Proteomic Analysis of the Lens Extracellular Diffusion Barrier.Investigative ophthalmology & visual science · 2021Article
- Ezrin Is a Novel Protein Partner of Aquaporin-5 in Human Salivary Glands and Shows Altered Expression and Cellular Localization in Sjögren's Syndrome.International journal of molecular sciences · 2021Article
- Changes to Zonular Tension Alters the Subcellular Distribution of AQP5 in Regions of Influx and Efflux of Water in the Rat Lens.Investigative ophthalmology & visual science · 2020Article
- Cleavage C-terminal to Asp leads to covalent crosslinking of long-lived human proteins.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability.Experimental eye research · 2019Article
- Spontaneous cross-linking of proteins at aspartate and asparagine residues is mediated via a succinimide intermediate.The Biochemical journal · 2018Article
- The Role of Aquaporins in Ocular Lens Homeostasis.International journal of molecular sciences · 2017Review
- Aquaporin Protein-Protein Interactions.International journal of molecular sciences · 2017Review
- Identification of a direct Aquaporin-0 binding site in the lens-specific cytoskeletal protein filensin.Experimental eye research · 2017Article
- The lens actin filament cytoskeleton: Diverse structures for complex functions.Experimental eye research · 2017Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
purposeAquaporin 0 (AQP0) is the major intrinsic protein in the lens and is essential for establishing proper fiber cell structure and organization. Cytoskeletal proteins that directly interact with the C terminus of AQP0 are identified herein.
methodsThe water-insoluble fraction of lens fiber cells was chemically cross-linked, and cross-linked peptides with the C terminus of AQP0 were identified by mass spectrometry. Coimmunoprecipitation and AQP0 C-terminal peptide pulldown experiments were used to confirm the protein-protein interaction.
resultsUnexpectedly, AQP0 was found to directly associate with ezrin/radixin/moesin (ERM) family members, proteins that are involved in linkage of actin filaments to the plasma membrane. Cross-linked peptides were detected between AQP0 and degenerate sequences of ezrin and radixin; however, AQP0 interaction with ezrin is believed to play a more significant function in the lens because of its higher level of expression and observed ezrin-specific cross-linking. The interaction was found to occur between the C terminus of AQP0 and subdomains F1 and F3 of ERM proteins. The interaction between AQP0 and ezrin was confirmed by coimmunoprecipitation and AQP0 C-terminal peptide pulldown experiments.
conclusionsConsidering the important known functions of the cellular actin cytoskeleton in fiber cell differentiation, the interaction of AQP0 and ERM proteins may play an important role in fiber cell morphology, elongation, and organization.
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