Immune Netw.  2002 Sep;2(3):137-141. 10.4110/in.2002.2.3.137.

Identification of a Variant Form of Cellular Inhibitor of Apoptosis Protein (c-IAP2) That Contains a Disrupted Ring Domain

• Park SM
• Kim JS
• Park JH
• Kang SG
• Lee TH

• KMID: 1571515
• DOI: http://doi.org/10.4110/in.2002.2.3.137

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.

Keyword

c-IAP2; TNF; NF-kappaB; TRAF2; TRAF6

MeSH Terms

Apoptosis
Humans
Inhibitor of Apoptosis Proteins*
NF-kappa B
TNF Receptor-Associated Factor 2
TNF Receptor-Associated Factor 6
Two-Hybrid System Techniques
Inhibitor of Apoptosis Proteins
NF-kappa B
TNF Receptor-Associated Factor 2
TNF Receptor-Associated Factor 6