Identification of a Variant Form of Cellular Inhibitor of Apoptosis Protein (c-IAP2) That Contains a Disrupted Ring Domain.
- Author:
Sun Mi PARK
1
;
Ji Su KIM
;
Ji Hyun PARK
;
Seung Goo KANG
;
Tae Ho LEE
Author Information
- Publication Type:Original Article
- Keywords: c-IAP2; TNF; NF-kappaB; TRAF2; TRAF6
- MeSH: Apoptosis; Humans; Inhibitor of Apoptosis Proteins*; NF-kappa B; TNF Receptor-Associated Factor 2; TNF Receptor-Associated Factor 6; Two-Hybrid System Techniques
- From:Immune Network 2002;2(3):137-141
- CountryRepublic of Korea
- Language:English
- 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.
