Abstract
The fiber cell of the vertebrate ocular lens assembles a cytoskeletal structure, the beaded filament, which contains two proteins unique to the fiber cell: CP49 (phakinin) and CP115/CP95 (filensin). We report here the complete primary sequence and gene structure for human CP49. These data show that CP49 is a member of the intermediate filament family, but highly unusual in several regards. 1) CP49 primary sequence does not permit unambiguous assignment to any existing class of intermediate filament protein, but exhibits a gene structure that is identical to the Type I cytokeratins. 2) CP49 essentially lacks one of the three major domains that characterize all intermediate filament proteins, the carboxyl-terminal tail domain. 3) CP49 shows substitutions at 3 of 4 residues in the otherwise highly conserved intermediate filament protein motif LNDR. Notably, this divergence includes an Arg to Cys substitution that has only been observed in the mutant human cytokeratin K14, a mutation shown to cause the skin blistering seen in the genetic disorder Dowling-Meara epidermolysis bullosa simplex.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 6729-6735 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 271 |
| Issue number | 12 |
| DOIs | |
| State | Published - Mar 22 1996 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Gene structure and cDNA sequence identify the beaded filament protein CP49 as a highly divergent type I intermediate filament protein. / Hess, John F.; Casselman, Jodi T.; FitzGerald, Paul G.
In: Journal of Biological Chemistry, Vol. 271, No. 12, 22.03.1996, p. 6729-6735.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Gene structure and cDNA sequence identify the beaded filament protein CP49 as a highly divergent type I intermediate filament protein
AU - Hess, John F.
AU - Casselman, Jodi T.
AU - FitzGerald, Paul G
PY - 1996/3/22
Y1 - 1996/3/22
N2 - The fiber cell of the vertebrate ocular lens assembles a cytoskeletal structure, the beaded filament, which contains two proteins unique to the fiber cell: CP49 (phakinin) and CP115/CP95 (filensin). We report here the complete primary sequence and gene structure for human CP49. These data show that CP49 is a member of the intermediate filament family, but highly unusual in several regards. 1) CP49 primary sequence does not permit unambiguous assignment to any existing class of intermediate filament protein, but exhibits a gene structure that is identical to the Type I cytokeratins. 2) CP49 essentially lacks one of the three major domains that characterize all intermediate filament proteins, the carboxyl-terminal tail domain. 3) CP49 shows substitutions at 3 of 4 residues in the otherwise highly conserved intermediate filament protein motif LNDR. Notably, this divergence includes an Arg to Cys substitution that has only been observed in the mutant human cytokeratin K14, a mutation shown to cause the skin blistering seen in the genetic disorder Dowling-Meara epidermolysis bullosa simplex.
AB - The fiber cell of the vertebrate ocular lens assembles a cytoskeletal structure, the beaded filament, which contains two proteins unique to the fiber cell: CP49 (phakinin) and CP115/CP95 (filensin). We report here the complete primary sequence and gene structure for human CP49. These data show that CP49 is a member of the intermediate filament family, but highly unusual in several regards. 1) CP49 primary sequence does not permit unambiguous assignment to any existing class of intermediate filament protein, but exhibits a gene structure that is identical to the Type I cytokeratins. 2) CP49 essentially lacks one of the three major domains that characterize all intermediate filament proteins, the carboxyl-terminal tail domain. 3) CP49 shows substitutions at 3 of 4 residues in the otherwise highly conserved intermediate filament protein motif LNDR. Notably, this divergence includes an Arg to Cys substitution that has only been observed in the mutant human cytokeratin K14, a mutation shown to cause the skin blistering seen in the genetic disorder Dowling-Meara epidermolysis bullosa simplex.
UR - http://www.scopus.com/inward/record.url?scp=0029911721&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029911721&partnerID=8YFLogxK
U2 - 10.1074/jbc.271.12.6729
DO - 10.1074/jbc.271.12.6729
M3 - Article
C2 - 8636093
AN - SCOPUS:0029911721
VL - 271
SP - 6729
EP - 6735
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 12
ER -