| Autor: |
Cui, Cunqi, Stambrook, Peter J., Parysek, Linda M. |
| Zdroj: |
Journal of Cell Science; October 1995, Vol. 108 Issue: 10 p3279-3284, 6p |
| Abstrakt: |
The properties of full-length and mutant peripherins were studied in intermediate filament-less SW13 cells to define regions of peripherin that are essential for initiation of filament assembly. A full-length rat peripherin gene transfected into SW13 cells resulted in filament formation, consistent with the close structural relationship of peripherin to other type III intermediate filament proteins that readily form homopolymers. Translation of full-length rat peripherin is initiated predominantly at the second of two inframe AUGs. Deletions within the amino terminus of wildtype peripherin abolished its ability to form filaments in SW13 cells. In contrast, deletion of the entire carboxylterminal tail of peripherin did not affect its ability to form filamentous arrays in transfected SW13 cells. These results indicate that, of the intermediate filament proteins that are expressed in mature neurons, only peripherin and αinternexin are capable of making homopolymer intermediate filaments. In addition, mutations of the carboxyl tail of peripherin generally do not interfere with filament network formation. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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