The mouse filensin gene: Structure and evolutionary relation to other intermediate filament genes

Fotini Gounari, Niki Karagianni, Antoaneta Mincheva, Peter Lichter, Spyros D. Georgatos, Volker Schirrmacher

Research output: Contribution to journalArticlepeer-review


Filensin and phakinin are two lens-specific members of the intermediate filament (IF) superfamily of proteins. They coassemble to form a beaded submembraneous filamentous network, the beaded filaments (BFs). The low sequence homology and differences in assembly compared to other IF proteins do not allow their classification in any of the five IF subgroups. The organization of the phakinin gene exon/intron boundaries provides evidence that this partner may be sharing a common origin with type I cytokeratin genes. Here we report the molecular cloning, sequence and characterization of the mouse filensin gene. The filensin gene consists of 8 exons and 7 introns, with 6 introns interrupting its rod domain in a highly conserved manner characteristic of type III IF genes, like vimentin, desmin, or peripherin. Of the two tail domain exons the one adjacent to the rod domain, compares to exon 7 of the non-neuronal cytoplasmic IF gene of helix aspersa and to the lamin region bridging the end of the rod domain to the nuclear localization signal. Altogether, these observations indicate that the lens beaded filaments form an independent class of IF.

Original languageEnglish (US)
Pages (from-to)371-378
Number of pages8
JournalFEBS Letters
Issue number2
StatePublished - Aug 18 1997


  • Beaded filaments
  • Intermediate filaments
  • Mouse filensin gene

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


Dive into the research topics of 'The mouse filensin gene: Structure and evolutionary relation to other intermediate filament genes'. Together they form a unique fingerprint.

Cite this