ArticleThe Journal of cell biology1993
Bovine filensin possesses primary and secondary structure similarity to intermediate filament proteins.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 89 citations in OpenAlex.
- 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
- Single cell transcriptomics of the developing zebrafish lens and identification of putative controllers of lens development.Experimental eye research · 2021Article
- Article
- Identification of a direct Aquaporin-0 binding site in the lens-specific cytoskeletal protein filensin.Experimental eye research · 2017Article
- Expression of the type VI intermediate filament proteins CP49 and filensin in the mouse lens epithelium.Molecular vision · 2016Article
- A novel terminal web-like structure in cortical lens fibers: architecture and functional assessment.Anatomical record (Hoboken, N.J. : 2007) · 2010Article
- Sef is a negative regulator of fiber cell differentiation in the ocular lens.Differentiation; research in biological diversity · 2010Article
- 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
- The structure of the cytoplasm of lens fibers as determined by conical tomography.Experimental eye research · 2009Article
- Periplakin interactions with lens intermediate and beaded filaments.Investigative ophthalmology & visual science · 2009Article
- Lens intermediate filaments.Experimental eye research · 2009Review
- The function of filensin and phakinin in lens transparency.Molecular vision · 2008Article
- Resisting the effects of aging: a function for the fiber cell beaded filament.Investigative ophthalmology & visual science · 2008Article
- Identifying the role of specific motifs in the lens fiber cell specific intermediate filament phakosin.Investigative ophthalmology & visual science · 2007Article
- Insights into the beaded filament of the eye lens.Experimental cell research · 2007Review
- Autosomal-dominant congenital cataract associated with a deletion mutation in the human beaded filament protein gene BFSP2.American journal of human genetics · 2000Article
- Characterization of the chicken transitin gene reveals a strong relationship to the nestin intermediate filament class.Journal of molecular neuroscience : MN · 1999Article
- Intermediate filaments as dynamic structures.Cancer metastasis reviews · 1996Review
- Implications of intermediate filament protein phosphorylation.Cancer metastasis reviews · 1996Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cDNA coding for calf filensin, a membrane-associated protein of the lens fiber cells, has been cloned and sequenced. The predicted 755-amino acid-long open reading frame shows primary and secondary structure similarity to intermediate filament (IF) proteins. Filensin can be divided into an NH2-terminal domain (head) of 38 amino acids, a middle domain (rod) of 279 amino acids, and a COOH-terminal domain (tail) of 438 amino acids. The head domain contains a di-arginine/aromatic amino acid motif which is also found in the head domains of various intermediate filament proteins and includes a potential protein kinase A phosphorylation site. By multiple alignment to all known IF protein sequences, the filensin rod, which is the shortest among IF proteins, can be subdivided into three subdomains (coils 1a, 1b, and 2). A 29 amino acid truncation in the coil 2 region accounts for the smaller size of this domain. The filensin tail contains 6 1/2 tandem repeats which match analogous motifs of mammalian neurofilament M and H proteins. We suggest that filensin is a novel IF protein which does not conform to any of the previously described classes. Purified filensin fails to form regular filaments in vitro (Merdes, A., M. Brunkener, H. Horstmann, and S. D. Georgatos. 1991. J. Cell Biol. 115:397-410), probably due to the missing segment in the coil 2 region. Participation of filensin in a filamentous network in vivo may be facilitated by an assembly partner.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.