CIPER, a Novel NF κB-activating Protein Containing a Caspase Recruitment Domain with Homology to Herpesvirus-2 Protein E10

Koseki, Takeyoshi; Inohara, Naohiro; Chen, Shu; Carrió, Roberto; Merino, Jesús; Hottiger, Michael O.; Nabel, Gary J.; Núñez, Gabriel

doi:10.1074/jbc.274.15.9955

Cited by 139 publications

(143 citation statements)

References 36 publications

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“…Therefore, it has been proposed that Bcl10 is a tumor suppressor gene. Overexpression of wild-type Bcl10 induces apoptosis in several types of cells (Thome et al, 1999;Koseki et al, 1999;. Indeed, our recent report showed that Bcl10 transgenic mouse revealed promotion of apoptosis in the thymocytes and lymphocytes at postnatal stages.…”

Section: Discussionmentioning

confidence: 99%

Interchangeable binding of Bcl10 to TRAF2 and cIAPs regulates apoptosis signaling

et al. 2001

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Bcl10 was identi®ed as a candidate gene responsible for low grade B cell lymphomas of mucosa-associated lymphoid tissue. Overexpression of Bcl10 in cultured cells was reported to promote apoptosis, however, the mechanism of regulation of apoptosis mediated by Bcl10 has not been demonstrated. In the present study, we analysed the apoptosis signaling pathway mediated by Bcl10, focusing on phosphorylation of Bcl10 and the dynamic interaction with its binding partners during apoptosis. Previously, we have demonstrated that Bcl10 potentially interacts with the other apoptosis regulator, TNF receptor associated factor-2 (TRAF2) and inhibitor of apoptosis proteins (cIAPs). The present results showed that the complex formation of these molecules was regulated by phosphorylation of Bcl10, that is, phosphorylation of Bcl10 resulted in binding of Bcl10 to cIAPs and the dissociation of it from TRAF2. Moreover, hyperphosphorylation of Bcl10 enhanced apoptosis, suggesting that changes in the binding partners of Bcl10 were correlated to the promotion of apoptosis as mediated by Bcl10. Indeed, the mutant which was deleted from the binding site of Bcl10 for cIAPs, could not induce apoptosis. These ®ndings indicate that Bcl10 is a mediator of apoptosis signaling, by switching over binding to cIAPs from TRAF2 through the events of Bcl10 phosphorylation. Oncogene (2001) 20, 4317 ± 4323.

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Section: Discussionmentioning

confidence: 99%

Interchangeable binding of Bcl10 to TRAF2 and cIAPs regulates apoptosis signaling

et al. 2001

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“…This protein was initially shown to be proapoptotic, 36 which was also isolated as a CARD-containing protein, with the aid of the protein database searches. [71][72][73][74] The CARD motif is found in a number of apoptotic regulatory proteins and allows for both homo-and heterodimerization of the CARD-containing proteins. Overexpression of BCL10 activates the I-kB kinase (IKK) complex through CARD domain-mediated self-oligomerization, resulting in NF-kB activation.…”

Section: Molecular Genetics Of Mucosa-associated Lymphoid Tissue Lympmentioning

confidence: 99%

Molecular pathogenesis of MALT lymphoma: two signaling pathways underlying the antiapoptotic effect of API2-MALT1 fusion protein

2006

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At least three recurrent chromosomal translocations, t(11;18)(q21;q21), t(1;14)(p22;q32), t(14;18)(q32;q21), involving the API2-MALT1 fusion protein, BCL10 and MALT1, have been implicated in the pathogenesis of mucosa-associated lymphoid tissue (MALT) lymphoma. Several lines of evidence indicated that both BCL10 and MALT1 are required for nuclear factor kappa B (NF-jB) activation by antigen receptor stimulation in lymphocytes, and API2-MALT1 can bypass this BCL10/MALT1 signaling pathway. Nuclear factor kappa B activation may contribute to antiapoptotic effect through NF-jB-mediated upregulation of apoptotic inhibitor genes. We recently demonstrated that API2-MALT1 can induce transactivation of the API2 gene through NF-jB activation, thus highlighting a positive feedback-loop mechanism of self-activation by upregulating its own expression in t(11;18) MALT lymphomas. We also demonstrated that API2-MALT1 possesses an antiapoptotic effect, in part, through its direct interaction with apoptotic regulators. These findings therefore led us to hypothesize that the antiapoptotic effect by API2-MALT1 may be mediated by its interaction with apoptotic regulators, on the one hand, and by NF-jB-mediated upregulation of apoptotic inhibitor genes on the other. We also found that BCL10 and MALT1 are shuttling between nucleus and cytoplasm, and that MALT1 can regulate the subcellular location of BCL10. Leukemia (2006) 20, 929-936.

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“…Bcl10 was identified by functional cloning from mucosa-associated lymphoid tissue (MALT) lymphoma cells [30,31] and by bioinformatics approaches as a CARD-containing protein [32][33][34]. Genetic studies using Bcl10-deficient mice have revealed that Bcl10 is an essential component in the T cell receptor (TCR)-and B cell receptor (BCR)-induced NF-κB activation, and functions downstream of PKC [29,35].…”

Section: Cbm Proteins In Antigen Receptor Signalingmentioning

confidence: 99%

NF-κB signaling pathways regulated by CARMA family of scaffold proteins

Blonska¹,

Lin²

2010

Cell Res

176

201

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The NF-κB family of transcription factors plays a crucial role in cell activation, survival and proliferation. Its aberrant activity results in cancer, immunodeficiency or autoimmune disorders. Over the past two decades, tremendous progress has been made in our understanding of the signals that regulate NF-κB activation, especially how scaffold proteins link different receptors to the NF-κB-activating complex, the IκB kinase complex. The growing number of these scaffolds underscores the complexity of the signaling networks in different cell types. In this review, we discuss the role of scaffold molecules in signaling cascades induced by stimulation of antigen receptors, G-protein-coupled receptors and C-type Lectin receptors, resulting in NF-κB activation. Especially, we focus on the family of Caspase recruitment domain (CARD)-containing proteins known as CARMA and their function in activation of NF-κB, as well as the link of these scaffolds to the development of various neoplastic diseases through regulation of NF-κB.

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CIPER, a Novel NF κB-activating Protein Containing a Caspase Recruitment Domain with Homology to Herpesvirus-2 Protein E10

Cited by 139 publications

References 36 publications

Interchangeable binding of Bcl10 to TRAF2 and cIAPs regulates apoptosis signaling

Interchangeable binding of Bcl10 to TRAF2 and cIAPs regulates apoptosis signaling

Molecular pathogenesis of MALT lymphoma: two signaling pathways underlying the antiapoptotic effect of API2-MALT1 fusion protein

NF-κB signaling pathways regulated by CARMA family of scaffold proteins

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