XIAP Induces NF-κB Activation via the BIR1/TAB1 Interaction and BIR1 Dimerization

Lu, Miao; Lin, Su Chang; Huang, Yihua; Kang, Young Jun; Rich, Rebecca L.; Lo, Yu Chih; Myszka, David G.; Han, Jiahuai; Wu, Hao

doi:10.1016/j.molcel.2007.05.006

Cited by 254 publications

(283 citation statements)

References 72 publications

(106 reference statements)

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“…However, in cIAP1 null myoblasts, in which levels of cIAP2 are barely detectable, I B␣ degradation was substantially attenuated. The related family member Xlinked IAP (XIAP) has also been previously implicated in NF-B signaling in some studies (24), and we therefore evaluated for its role in TNF␣-mediated NF-B activation. Unlike cIAP1 knockdown, siRNA targeting of XIAP had no bearing on TNF␣-mediated NF-B activation (Fig.…”

Section: S O L T a H E A R T S P L E E N L Iv E R B Rmentioning

confidence: 99%

Both cIAP1 and cIAP2 regulate TNFα-mediated NF-κB activation

Mahoney

Cheung

Mrad

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

480

410

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The cellular inhibitor of apoptosis 1 and 2 (cIAP1 and cIAP2) proteins have been implicated in the activation of NF-B by TNF␣; however, genetic deletion of either cIAP1 or 2 did not support a physiologically relevant role, perhaps because of functional redundancy. To address this, we used combined genetic and siRNA knockdown approaches and report that cIAP1 and 2 are indeed critical, yet redundant, regulators of NF-B activation upon TNF␣ treatment. Whereas NF-B was properly activated by TNF␣ in cultured and primary cells deficient in either cIAP1 or 2, removal of both cIAPs severely blunted its activation. After treatment with TNF␣, cIAP1 and 2 were rapidly recruited to the TNF receptor 1, along with the adapter protein TNF receptor associated factor 2. Importantly, either cIAP1 or 2 was required for proper TNF receptor 1 signalosome function. In their combined absence, polyubiquitination of receptor interacting protein 1, an upstream event necessary for NF-B signaling, was attenuated. As a result, phosphorylation of the inhibitor of B kinase ␤ was diminished, and signal transduction was severely blunted. Consequently, cells missing both cIAP1 and 2 were sensitized to TNF␣-mediated apoptosis.Collectively, these data demonstrate that either cIAP1 or 2 is required for proper Rip1 polyubiquitination and NF-B activation upon TNF␣ treatment.apoptosis ͉ Receptor Interacting Protein (RIP1)

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Section: S O L T a H E A R T S P L E E N L Iv E R B Rmentioning

confidence: 99%

Both cIAP1 and cIAP2 regulate TNFα-mediated NF-κB activation

Mahoney

Cheung

Mrad

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

480

410

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“…BIR1 facilitates binding of XIAP to the TGFb-activated kinase binding protein 1 (TAB1), thereby mediating activation of NFkB. 81 In contrast, the BIR2/BIR3 domains mediate binding of XIAP to proteins harbouring an IAP-binding motif, including active caspases. This interaction is facilitated by a deep hydrophobic peptide-binding groove within the BIR2 and BIR3.…”

Section: Xiap and Type 1 Versus Type 2 Fas-induced Apoptosis Signallingmentioning

confidence: 99%

Fas death receptor signalling: roles of Bid and XIAP

2011

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Fas (also called CD95 or APO-1), a member of a subgroup of the tumour necrosis factor receptor superfamily that contain an intracellular death domain, can initiate apoptosis signalling and has a critical role in the regulation of the immune system. Fas-induced apoptosis requires recruitment and activation of the initiator caspase, caspase-8 (in humans also caspase-10), within the death-inducing signalling complex. In so-called type 1 cells, proteolytic activation of effector caspases (-3 and -7) by caspase-8 suffices for efficient apoptosis induction. In so-called type 2 cells, however, killing requires amplification of the caspase cascade. This can be achieved through caspase-8-mediated proteolytic activation of the pro-apoptotic Bcl-2 homology domain (BH)3-only protein BH3-interacting domain death agonist (Bid), which then causes mitochondrial outer membrane permeabilisation. This in turn leads to mitochondrial release of apoptogenic proteins, such as cytochrome c and, pertinent for Fas death receptor (DR)-induced apoptosis, Smac/DIABLO (second mitochondria-derived activator of caspase/direct IAP binding protein with low Pi), an antagonist of X-linked inhibitor of apoptosis (XIAP), which imposes a brake on effector caspases. In this review, written in honour of Juerg Tschopp who contributed so much to research on cell death and immunology, we discuss the functions of Bid and XIAP in the control of Fas DR-induced apoptosis signalling, and we speculate on how this knowledge could be exploited to develop novel regimes for treatment of cancer. (FasL) can induce apoptosis by a mechanism involving the adaptor protein FADD (Fas-associating protein with a novel death domain) and the proximal initiator caspase, caspase-8 (and in humans also caspase-10). Apoptosis can only be triggered by the membrane-bound form of FasL. Caspase-8 can activate the Bcl-2 homology (BH)3-only protein BH3-interacting domain death agonist (Bid), enabling a crosstalk to the intrinsic apoptotic pathway. Whereas FasL-stimulated type I cells can die independently of the intrinsic apoptotic machinery, type II cells depend on this crosstalk to mitochondria. X-linked inhibitor of apoptosis (XIAP) directly inhibits effector caspases and constitutes a discriminator between the type I and the type II Fas-induced apoptosis signalling. Besides apoptosis, Fas can trigger several non-apoptotic signalling pathways, including RIP1 kinase-dependent cell death (necroptosis), when caspase-8 is missing or disabled, as well as pathways that promote cell activation and cell proliferation. Open QuestionsHow is Fas-induced necroptosis and proliferation regulated at the molecular level? What is the role of XIAP's RING domain in Fas signalling? Why are certain Fas-expressing cell types refractory to FasL-induced killing? What are the roles of soluble FasL?The Death Receptor Fas Fas (also called CD95 or APO-1) is a member of the tumour necrosis factor receptor (TNF-R) superfamily, which also includes receptors for TNFa, TRAIL (TNF-related apoptosisinducing ligand), r...

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“…In fact, x-linked inhibitor of apoptosis protein (XIAP) is an upstream mediator of TAK1 signaling by DNA damage, TGF-b, and hypoxia (Figs. 3B, 3D, and 3F), and the crystal structure of a XIAP-TAB1 fragment has been solved (20). In addition, post-translational modification of TAB1 by phosphorylation can modulate TAK1 activity (21).…”

Section: Tab1 and Tak1 Activitymentioning

confidence: 99%

“…Injection of XIAP (or TAK1) into Xenopus embryos causes the ventralization of cells, thus mimicking TGF-b stimulation (46,47). The baculovirus IAP repeat (BIR1) domain of XIAP in complex with TAB1 has been solved by Xray crystallography, and this interaction is required for XIAP induction of TAK1 activation (20). In fact, overexpression of the BIR1 domain of XIAP can lead to NF-jB activation by TAK1 (20).…”

Section: Tak1 In the Tgf-b And Bmp Signaling Pathwaymentioning

confidence: 99%

TAK1, more than just innate immunity

et al. 2012

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SummaryTransforming growth factor b-activated kinase 1 (TAK1) is a key regulator of the innate immunity and the proinflammatory signaling pathway. In response to interleukin-1, tumor necrosis factor-a, and toll-like receptor agonists, it mediates the activation of the nuclear factor jB (NF-jB), c-Jun N-terminal kinase (JNK), and p38 pathways. In addition, TAK1 plays a central role in adaptive immunity, in which it mediates signaling from T-and B-cell receptors. This review will focus on recent developments and also examine the regulation of TAK1 in response to a diverse range of other stimuli including DNA damage, transforming growth factor-b, Wnt, osmotic stress, and hypoxia.2012 IUBMB IUBMB Life, 64(10): [825][826][827][828][829][830][831][832][833][834] 2012

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XIAP Induces NF-κB Activation via the BIR1/TAB1 Interaction and BIR1 Dimerization

Cited by 254 publications

References 72 publications

Both cIAP1 and cIAP2 regulate TNFα-mediated NF-κB activation

Both cIAP1 and cIAP2 regulate TNFα-mediated NF-κB activation

Fas death receptor signalling: roles of Bid and XIAP

TAK1, more than just innate immunity

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