T2BP, a Novel TRAF2 Binding Protein, Can Activate NF-κB and AP-1 without TNF Stimulation

Kanamori, Mutsumi; Suzuki, Harukazu; Saito, Rintaro; Muramatsu, Masami; Hayashizaki, Yoshihide

doi:10.1006/bbrc.2001.6315

Cited by 61 publications

(64 citation statements)

References 31 publications

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“…We identified a cDNA encoding a 184-amino acid protein, identical to T2BP previously identified as a TRAF2-binding protein, that activates NFB and JNK in transient transfection assays (Ref. 18 and data not shown). Because the present study showed that T2BP associates with TRAF6 and a forkhead-associated (FHA) domain of the T2BP (Fig.…”

Section: Identification Of Tifa As a Traf6-interacting Protein-tomentioning

confidence: 83%

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Identification of TIFA as an Adapter Protein That Links Tumor Necrosis Factor Receptor-associated Factor 6 (TRAF6) to Interleukin-1 (IL-1) Receptor-associated Kinase-1 (IRAK-1) in IL-1 Receptor Signaling

Takatsuna

Kato

Gohda

et al. 2003

Journal of Biological Chemistry

109

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Section: Identification Of Tifa As a Traf6-interacting Protein-tomentioning

confidence: 83%

“…Thus, TIFA may function in innate immunity. Although T2BP, identical to TIFA, was shown to associate with TRAF2, when they overexpressed, the T2BP/ TRAF2 interaction in vivo has never been demonstrated (18). Nevertheless, TIFA may regulate both TRAF2 and TRAF6 in vivo.…”

Section: Discussionmentioning

confidence: 99%

Identification of TIFA as an Adapter Protein That Links Tumor Necrosis Factor Receptor-associated Factor 6 (TRAF6) to Interleukin-1 (IL-1) Receptor-associated Kinase-1 (IRAK-1) in IL-1 Receptor Signaling

Takatsuna

Kato

Gohda

et al. 2003

Journal of Biological Chemistry

109

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“…Endogenous TIFA constitutively associates with TRAF6, whereas it only interacts with IRAK-1 upon IL-1 stimulation [51]. In addition, overexpression of TIFA induces NF-kB and JNK activation in HEK293 cells [52]. Lysine 124 in TRAF6 was identified as the main ubiquitin acceptor site for auto-ubiquitination, and mutation of this lysine leads to impaired TAK1, IKK and JNK activation [22].…”

Section: Il-1r and Tlr-4 Signaling To Nf-kbmentioning

confidence: 99%

TLR-4, IL-1R and TNF-R signaling to NF-κB: variations on a common theme

Verstrepen

Bekaert

Chau

et al. 2008

Cell. Mol. Life Sci.

393

297

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Abstract. Toll-like receptors (TLRs) as well as the receptors for tumor necrosis factor (TNF-R) and interleukin-1 (IL-1R) play an important role in innate immunity by regulating the activity of distinct transcription factors such as nuclear factor-kB (NF-kB). TLR, IL-1R and TNF-R signaling to NF-kB converge on a common IkB kinase complex that phosphorylates the NF-kB inhibitory protein IkBa. However, upstream signaling components are in large part receptor-specific. Nevertheless, the principles of signaling are similar, involving the recruitment of specific adaptor proteins and the activation of kinase cascades in which protein-protein interactions are controlled by poly-ubiquitination. In this review, we will discuss our current knowledge of NF-kB signaling in response to TLR-4, TNF-R and IL-1R stimulation, with a special focus on the similarities and dissimilarities among these pathways.Keywords. Toll-like receptor 4, interleukin-1, tumor necrosis factor, NF-kB, signal transduction. NF-kB, does it still need to be introduced?Nuclear factor kB (NF-kB) is the generic name of a family of transcription factors that regulate the expression of a large number of genes involved in immune and inflammatory responses, as well as in cell survival, cell proliferation and cell differentiation. NFkB transcription factors are activated in response to various stimuli, including cytokines, infectious agents, injury and other stressful conditions requiring rapid reprogramming of gene expression. Inappropriate activation of the NF-kB signaling pathway is implicated in the pathogenesis of chronic inflammation and autoimmunity, certain hereditary disorders and various cancers. In mammals, the NF-kB family consists of five proteins sharing a highly conserved Rel homology domain: c-Rel, RelB, p65 (= RelA), p105 (= NF-kB1) and p100 (=NF-kB2). The first three contain Cterminal transactivation domains, while the others share a long C-terminal domain with multiple copies of ankyrin repeats, which inhibit their activation.

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“…The two T2BPs found in human and mouse are relatively small proteins of 184 amino acids, both of which have a forkhead-associated domain, namely a phosphopeptide binding motif. The co-immunoprecipitation analysis showed that T2BPs interact with the TRAF domain of TRAF2 (Kanamori et al, 2002).…”

Section: Introductionmentioning

confidence: 98%

“…Several proteins that interact with TRAF2 have been identified by two-hybrid screening and co-immunoprecipitation ), among which a TRAF2 binding protein (T2BP) was found by a two-hybrid screening as a novel TRAF2 interacting protein with roles in the activation of NF kB and activator protein-1 (AP-1) (Kanamori et al, 2002). To date, T2BP homologues have been reported only in human and mouse (Kanamori et al, 2002;Matsuda et al, 2003). The two T2BPs found in human and mouse are relatively small proteins of 184 amino acids, both of which have a forkhead-associated domain, namely a phosphopeptide binding motif.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning of TRAF2 binding protein gene and its promoter region from the grass carp Ctenopharyngodon idellus

Chang¹,

Nie²,

Sun³

et al. 2005

Veterinary Immunology and Immunopathology

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T2BP, a Novel TRAF2 Binding Protein, Can Activate NF-κB and AP-1 without TNF Stimulation

Cited by 61 publications

References 31 publications

Identification of TIFA as an Adapter Protein That Links Tumor Necrosis Factor Receptor-associated Factor 6 (TRAF6) to Interleukin-1 (IL-1) Receptor-associated Kinase-1 (IRAK-1) in IL-1 Receptor Signaling

Identification of TIFA as an Adapter Protein That Links Tumor Necrosis Factor Receptor-associated Factor 6 (TRAF6) to Interleukin-1 (IL-1) Receptor-associated Kinase-1 (IRAK-1) in IL-1 Receptor Signaling

TLR-4, IL-1R and TNF-R signaling to NF-κB: variations on a common theme

Molecular cloning of TRAF2 binding protein gene and its promoter region from the grass carp Ctenopharyngodon idellus

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