Identification of a Variant Form of Cellular Inhibitor of Apoptosis Protein (c-IAP2) That Contains a Disrupted Ring Domain
Immune Network
; : 137-141, 2002.
Article
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| WPRIM
| ID: wpr-134612
Biblioteca responsable:
WPRO
ABSTRACT
Among the members of the inhibitor of apoptosis (IAP) protein family, only Livin and survivin have been reported to have variant forms. We have found a variant form of c-IAP2 through the interaction with the X protein of HBV using the yeast two-hybrid system. In contrast to the wild-type c-IAP2, the variant form has two stretches of sequence in the RING domain that are repeated in the C-terminus that would disrupt the RING domain. We demonstrate that the variant form has an inhibitory effect on TNF-mediated NF-kappaB activation unlike the wild-type c-IAP2, which increases TNF- mediated NF-kappaB activation. These results suggest that this variant form has different activities from the wild-type and the RING domain may be involved in the regulation of TNF-induced NF-kappaB activation.
Palabras clave
Texto completo:
1
Índice:
WPRIM
Asunto principal:
FN-kappa B
/
Apoptosis
/
Técnicas del Sistema de Dos Híbridos
/
Factor 2 Asociado a Receptor de TNF
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Factor 6 Asociado a Receptor de TNF
/
Proteínas Inhibidoras de la Apoptosis
Tipo de estudio:
Diagnostic_studies
/
Prognostic_studies
Límite:
Humans
Idioma:
En
Revista:
Immune Network
Año:
2002
Tipo del documento:
Article