TY - JOUR
T1 - The mouse filensin gene
T2 - Structure and evolutionary relation to other intermediate filament genes
AU - Gounari, Fotini
AU - Karagianni, Niki
AU - Mincheva, Antoaneta
AU - Lichter, Peter
AU - Georgatos, Spyros D.
AU - Schirrmacher, Volker
N1 - Funding Information:
F. Gounari was supported by a `habilitations stipendium' from the Deutsche Forschungs Gemeinshaft. The authors would like to thank Mr. E. Rezavandy and Ms. A. Lichtenauer for excelent technical assistance. The authors would like to particularly thank Dr. K. Khazaie for continuous support and encouragement.
PY - 1997/8/18
Y1 - 1997/8/18
N2 - 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.
AB - 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.
KW - Beaded filaments
KW - Intermediate filaments
KW - Mouse filensin gene
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U2 - 10.1016/S0014-5793(97)00937-X
DO - 10.1016/S0014-5793(97)00937-X
M3 - Article
C2 - 9280315
AN - SCOPUS:0030757156
SN - 0014-5793
VL - 413
SP - 371
EP - 378
JO - FEBS Letters
JF - FEBS Letters
IS - 2
ER -