ArticleInvestigative ophthalmology & visual science2010
Posttranslational modifications of the bovine lens beaded filament proteins filensin and CP49.
Article in Investigative ophthalmology & visual science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 25 citations in OpenAlex.
- 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
- Lens Aquaporins in Health and Disease: Location is Everything!Frontiers in physiology · 2022Review
- Proteomic characterization of the human lens and Cataractogenesis.Expert review of proteomics · 2021Review
- 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
- A predominant form of C-terminally end-cleaved AQP0 functions as an open water channel and an adhesion protein in AQP0Biochemical and biophysical research communications · 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
- DehydroalanylGly, a new post translational modification resulting from the breakdown of glutathione.Biochimica et biophysica acta. General subjects · 2018Article
- Identification of a direct Aquaporin-0 binding site in the lens-specific cytoskeletal protein filensin.Experimental eye research · 2017Article
- Identification and Functional Assessment of Age-Dependent Truncations to Cx46 and Cx50 in the Human Lens.Investigative ophthalmology & visual science · 2016Article
- Spatially Directed Proteomics of the Human Lens Outer Cortex Reveals an Intermediate Filament Switch Associated With the Remodeling Zone.Investigative ophthalmology & visual science · 2016Article
- 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
- Lens β-crystallins: the role of deamidation and related modifications in aging and cataract.Progress in biophysics and molecular biology · 2014Review
- Human protein aging: modification and crosslinking through dehydroalanine and dehydrobutyrine intermediates.Aging cell · 2014Article
- Proteomics and phosphoproteomics analysis of human lens fiber cell membranes.Investigative ophthalmology & visual science · 2013Article
- Electron tomography of fiber cell cytoplasm and dense cores of multilamellar bodies from human age-related nuclear cataracts.Experimental eye research · 2012Article
- Aquaporin-0 interacts with the FERM domain of ezrin/radixin/moesin proteins in the ocular lens.Investigative ophthalmology & visual science · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
purposeThe lens beaded filament proteins filensin and CP49 are phosphorylated proteins that undergo proteolytic degradation with fiber cell age; however, the specific sites of modifications remain largely unknown. The purpose of this study was to identify posttranslational modifications (PTMs) in bovine lens beaded filament proteins.
methodsFilensin and CP49 were enriched by urea extraction of lens fiber cell homogenates after the water-soluble fraction was removed. The urea-soluble fraction was separated by SDS-PAGE, and the corresponding filensin and CP49 bands were digested by trypsin, Lys C, or Glu C. The enzymatic digests were analyzed by HPLC mass spectrometry.
resultsThe sequences of lens beaded filament proteins were systematically mapped, and putative database sequence errors of filensin were identified. The data also indicated that Met-1 of CP49 was removed and Ser2 was acetylated. Nine phosphorylation sites on filensin and seven phosphorylation sites on CP49 were identified. Filensin was found to be truncated at D431 and L39, and the resulting new N termini were N-myristoylated and N-acetylated, respectively. Truncation of CP49 occurred at D37. Aspartic acid isomerization to isoaspartic acid occurs at the major truncation sites of filensin (D431) and of CP49 (D37).
conclusionsThis study identified sites of phosphorylation and truncation in filensin and CP49 and revealed two unusual PTMs: postproteolytic N-acetylation and N-myristoylation of filensin. The detailed knowledge about these PTMs provides important information for further study of their functional consequences-for example protein redistribution during lens fiber cell differentiation and aging.
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