ArticleThe Journal of cell biology1991
Filensin: a new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell.
Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 97 citations in OpenAlex.
- The Human Lens Fiber Cytoskeletome Reveals Neuronal Signatures and the Presence of Chaperonins, Proteasome, Signaling, and Redox Regulators.Investigative ophthalmology & visual science · 2026Article
- 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
- Update of the keratin gene family: evolution, tissue-specific expression patterns, and relevance to clinical disorders.Human genomics · 2022Article
- Quantitative Phosphoproteomic Comparison of Lens Proteins in Highly Myopic Cataract and Age-Related Cataract.BioMed research international · 2021Article
- Identification of a direct Aquaporin-0 binding site in the lens-specific cytoskeletal protein filensin.Experimental eye research · 2017Article
- α6 integrin transactivates insulin-like growth factor receptor-1 (IGF-1R) to regulate caspase-3-mediated lens epithelial cell differentiation initiation.The Journal of biological chemistry · 2014Article
- Derivation of multiple cranial tissues and isolation of lens epithelium-like cells from human embryonic stem cells.Stem cells translational medicine · 2013Article
- Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types.Cytoskeleton (Hoboken, N.J.) · 2012Review
- Periaxin is required for hexagonal geometry and membrane organization of mature lens fibers.Developmental biology · 2011Article
- The effect of the interaction between aquaporin 0 (AQP0) and the filensin tail region on AQP0 water permeability.Molecular vision · 2011Article
- Posttranslational modifications of the bovine lens beaded filament proteins filensin and CP49.Investigative ophthalmology & visual science · 2010Article
- Functions of the intermediate filament cytoskeleton in the eye lens.The Journal of clinical investigation · 2009Review
- Calpain expression and activity during lens fiber cell differentiation.The Journal of biological chemistry · 2009Article
- The structure of the cytoplasm of lens fibers as determined by conical tomography.Experimental eye research · 2009Article
- Identification of a novel intermediate filament-linked N-cadherin/gamma-catenin complex involved in the establishment of the cytoarchitecture of differentiated lens fiber cells.Developmental biology · 2008Article
- The function of filensin and phakinin in lens transparency.Molecular vision · 2008Article
- Insights into the beaded filament of the eye lens.Experimental cell research · 2007Review
- Intermediate filaments: a historical perspective.Experimental cell research · 2007Review
- Article
- Integrating the actin and vimentin cytoskeletons. adhesion-dependent formation of fimbrin-vimentin complexes in macrophages.The Journal of cell biology · 1999Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have studied the molecular properties of a 100-kD protein, termed filensin, which we have isolated from porcine lens membranes. Filensin represents a membrane-associated element, resistant to salt and nonionic detergent treatment, and extractable only by alkali or high concentrations of urea. By indirect immunofluorescence and immunoelectron microscopy, this protein can be localized at the periphery of the lens fiber cells. Immunochemical analysis suggests that filensin originates from a larger 110-kD component which is abundantly expressed in lens but not in other tissues. Purified filensin polymerizes in a salt-dependent fashion and forms irregular fibrils (integral of 10 nm in diameter) when reconstituted into buffers of physiological ionic strength and neutral pH. Radiolabeled filensin binds specifically to lens vimentin under isotonic conditions, as demonstrated by affinity chromatography and ligand-blotting assays. By the latter approach, filensin also reacts with a 47-kD peripheral membrane protein of the lens cells. Purified filensin binds to PI, a synthetic peptide modelled after a segment of the COOH-terminal domain of peripherin (a type III intermediate filament protein highly homologous to vimentin), but not to various other peptides including the NH2-terminal headpiece of vimentin and derivatives of its middle (rod) domain. The filensin-PI binding is inhibited by purified lamin B, which is known to interact in vitro with PI (Djabali, K., M.-M. Portier, F. Gros, G. Blobel, and S. D. Georgatos. 1991. Cell. 64:109-121). Finally, limited proteolysis indicates that the filensin-vimentin interaction involves a 30-kD segment of the filensin molecule. Based on these observations, we postulate that the lens fiber cells express a polymerization-competent protein which is tightly associated with the plasma membrane and has the potential to serve as an anchorage site for vimentin intermediate filaments.
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