Dissecting processing and apoptotic activity of a cysteine protease by mutant analysis.
J Cell Biol
; 135(2): 479-86, 1996 Oct.
Article
en En
| MEDLINE
| ID: mdl-8896603
ABSTRACT
We have compared the behavior of wild-type mouse NEDD-2, a neural precursor cell-expressed, developmentally down-regulated cysteine protease gene, to various mutant forms of the gene in both apoptotic activity in neuronal cells and proteolytic cleavage in the Semliki Forest virus and rabbit reticulocyte protein expression systems. Our results confirm that NEDD-2 processing and apoptotic activity are linked phenomena. They identify aspartate residues as likely targets for autocatalytic cleavage. They establish that cleavage events only occur at specific sites. Finally, they pinpoint differential effects of individual mutations on the overall proteolytic cleavage patterns, raising interesting questions related to the mechanisms of subunit assembly.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Cisteína Endopeptidasas
/
Proteínas
/
Apoptosis
/
Caspasas
/
Neuronas
Límite:
Animals
Idioma:
En
Revista:
J Cell Biol
Año:
1996
Tipo del documento:
Article
País de afiliación:
Suiza