ArticleExperimental eye research2017
Identification of a direct Aquaporin-0 binding site in the lens-specific cytoskeletal protein filensin.
Article in Experimental eye research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 20 citations in OpenAlex.
- CLIP2: a novel functional player in AQP5 trafficking dynamics and implications for Sjögren's disease.Cell communication and signaling : CCS · 2025Article
- Endogenous Aquaporin-0 Lipid Binding in Ocular Lens Tissue via Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025Article
- Aquaporin-0-protein interactions elucidated by crosslinking mass spectrometry.Biochemical and biophysical research communications · 2024Article
- Effects of truncations in the N- and C-terminal domains of filensin on filament formation with phakinin in cell-free conditions and cultured cells.FEBS open bio · 2023Article
- Article
- Methods for studying mammalian aquaporin biology.Biology methods & protocols · 2023Review
- Insights into the biochemical and biophysical mechanisms mediating the longevity of the transparent optics of the eye lens.The Journal of biological chemistry · 2022Review
- 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
- Article
- Deletion of beaded filament proteins or the C-terminal end of Aquaporin 0 causes analogous abnormal distortion aberrations in mouse lens.Experimental eye research · 2021Article
- Localization of the lens intermediate filament switch by imaging mass spectrometry.Experimental eye research · 2020Article
- Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.Progress in retinal and eye research · 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
- Deletion of Seventeen Amino Acids at the C-Terminal End of Aquaporin 0 Causes Distortion Aberration and Cataract in the Lenses of AQP0ΔC/ΔC Mice.Investigative ophthalmology & visual science · 2019Article
- Proteomic Analysis of S-Palmitoylated Proteins in Ocular Lens Reveals Palmitoylation of AQP5 and MP20.Investigative ophthalmology & visual science · 2018Article
- Yale School of Public Health Symposium on tissue imaging mass spectrometry: illuminating phenotypic heterogeneity and drug disposition at the molecular level.Human genomics · 2018Article
- The Role of Aquaporins in Ocular Lens Homeostasis.International journal of molecular sciences · 2017Review
- Aquaporin 0 Modulates Lens Gap Junctions in the Presence of Lens-Specific Beaded Filament Proteins.Investigative ophthalmology & visual science · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
An interaction between the C-terminus of aquaporin-0 (AQP0) and lens beaded filament protein filensin has been reported previously; however, the region of filensin that is involved in the interaction has not been determined. This study is designed to identify the region of filensin that interacts with AQP0. Chemical crosslinking coupled with mass spectrometry was used to identify the site of interaction. The protein complex was crosslinked with zero-length crosslinker: 1-Ethyl-3-[3-dimethylaminopropyl]carbodiimide Hydrochloride (EDC). The crosslinked membrane fraction was digested by trypsin and crosslinked peptides were identified by liquid chromatography-tandem mass spectrometry. A crosslinked peptide between bovine filensin 450-465 (VKGPKEPEPPADLYTK) and bovine AQP0 239-259 (GSRPSESNGQPEVTGEPVELK) was detected. AQP0/filensin crosslinking was not detected in superficial young fiber cells, but increased with fiber cell age in the lens cortex. AQP0/filensin crosslinking and filensin truncation were observed in the same regions of the lens. This crosslinked peptide can be detected in 75 kDa gel band confirming that AQP0/filensin crosslinking can occur between AQP0 and the filensin C-terminal fragment. These results suggest that the AQP0 C-terminus directly interacts with the region of filensin that is adjacent to the major truncation site and the polybasic cluster of residues in the filensin C-terminal tail. This interaction occurs in a specific region of the lens and could only occur between AQP0 and filensin C-terminal fragment in vivo. This interaction supports the dual roles of filensin in the lens; roles that could be important during lens development.
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