X-linked inhibitor of apoptosis (XIAP)-associated factor 1 (XAF1) is a cytokine-regulated, tumor necrosis factor (TNF) receptor-associated factor (TRAF) domain-containing protein that has a poorly defined cellular function.

XIAP (X-linked IAP) is the only family member that suppresses apoptosis by directly binding to and inhibiting caspases. On the other hand, cIAPs suppress the activation of the extrinsic apoptotic pathway by preventing the formation of pro-apoptotic signaling complexes.

Nov 18, 2022 · Our TRAF2 interactome analysis showed that cIAP1 was critical for TRAF2 to bind to its protein partners. Thus, cIAP1 and TRAF2 would be two essential subunits of a signaling complex promoting a...

Apr 4, 2010 · TRAF1/2 and cIAP1/2 are members of the TNF receptor associated factor (TRAF) and the inhibitor of apoptosis (IAP) families, respectively. They are critical for both the canonical and the noncanonical NF-κB signaling pathways.

Here we discuss the evidence implicating the RING domain of XIAP in the ubiquitin-mediated regulation of three somewhat arbitrarily divided categories of substrate: XIAP itself, XIAP-interacting proteins involved in apoptosis, and other targets whose physiologic roles likely extend beyond cell death.

Jan 4, 1999 · The human X‐chromosome‐linked inhibitor of apoptosis protein (XIAP) was isolated as a TAB1‐binding protein. XIAP associated not only with TAB1 but also with the BMP receptors in mammalian cells. Injection of XIAP mRNA into dorsal blastomeres enhanced the ventralization of Xenopus embryos in a TAB1–TAK1‐dependent manner. Furthermore, a ...

X-linked inhibitor of apoptosis (XIAP)-associated factor 1 (XAF1) is a cytokine-regulated, tumor necrosis factor (TNF) receptor-associated factor (TRAF) domain-containing protein that has a poorly defined cellular function.

The multiple biological activities of XIAP, its unique translational and post-translational control and the centrality of the caspase cascade make the control of XIAP expression an exceptionally promising molecular target for modulating apoptosis.

Expression of XIAP leads to increased nuclear translocation of the p65 subunit of NF-κB via a novel signaling pathway that involves the mitogen-activated protein kinase kinase kinase TAK1. We show that TAK1 physically interacts with NIK and with IKK2, and both XIAP or active TAK1 can stimulate IKK2 kinase activity.

X-linked inhibitor of apoptosis (XIAP)-associated factor 1 (XAF1) is a cytokine-regulated, tumor necrosis factor (TNF) receptor-associated factor (TRAF) domain-containing protein that has a poorly defined cellular function.