CLAP, a Novel Caspase Recruitment Domain-containing Protein in the Tumor Necrosis Factor Receptor Pathway, Regulates NF-κB Activation and Apoptosis

Srinivasula, Srinivasa M.; Ahmad, Manzoor; Lin, Jun-Hsiang; Poyet, Jean-Luc; Fernandes-Alnemri, Teresa; Tsichlis, Philip N.; Alnemri, Emad S.

doi:10.1074/jbc.274.25.17946

Cited by 107 publications

(96 citation statements)

References 65 publications

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“…Our laboratory had shown that a truncated Bcl10 protein consisting of only the N-terminal CARD (amino acids 1-103) plus the adjoining 16 amino acids of C-terminal sequence (amino acids 104 -119) was active at inducing NF-B (6). Others, however, had shown that the CARD alone was ineffectual (9). These results suggested that the region of Bcl10 between amino acids 104 and 119 is critically important for NF-B activation.…”

Section: Resultsmentioning

confidence: 75%

Bcl10 and MALT1, Independent Targets of Chromosomal Translocation in MALT Lymphoma, Cooperate in a Novel NF-κB Signaling Pathway

Lucas¹,

Yonezumi

Inohara³

et al. 2001

Journal of Biological Chemistry

394

392

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At least two distinct recurrent chromosomal translocations have been implicated in the pathogenesis of MALT lymphoma. The first, t(1;14), results in the transfer of the entire Bcl10 gene to chromosome 14 wherein Bcl10 expression is inappropriately stimulated by the neighboring Ig enhancer. The second, t(11;18), results in the synthesis of a novel fusion protein, API2-MALT1. Until now, no common mechanism of action has been proposed to explain how the products of these seemingly unrelated translocations may contribute to the same malignant process. We show here that Bcl10 and MALT1 form a strong and specific complex within the cell, and that these proteins synergize in the activation of NF-B. The data support a mechanism of action whereby Bcl10 mediates the oligomerization and activation of the MALT1 caspase-like domain. This subsequently activates the IKK complex through an unknown mechanism, setting in motion a cascade of events leading to NF-B induction. Furthermore, the API2-MALT1 fusion protein also strongly activates NF-B and shows dependence upon the same downstream signaling factors. We propose a model whereby both the Bcl10⅐MALT1 complex and the API2-MALT1 fusion protein activate a common downstream signaling pathway that originates with the oligomerization-dependent activation of the MALT1 caspase-like domain.

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Section: Resultsmentioning

confidence: 75%

Bcl10 and MALT1, Independent Targets of Chromosomal Translocation in MALT Lymphoma, Cooperate in a Novel NF-κB Signaling Pathway

Lucas¹,

Yonezumi

Inohara³

et al. 2001

Journal of Biological Chemistry

394

392

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“…That is, how does the TNFR1-TRADD-RIP1 complex stimulate the IKK complex? A recently identi®ed protein, CLAP (CARD-like apoptotic protein) (Srinivasula et al, 1999) (also called BCL-10/CIPER/c-E10/ CARMEN) (Costanzo et al, 1999;Koseki et al, 1999;Thome et al, 1999;Willis et al, 1999;Zhang et al, 1999), could ful®ll this role. The CLAP protein has two domains: a The examples in the list above are ones that have shown a direct functional involvement of NF-kB in the apoptotic response either by manipulating it pharmacologically or genetically.…”

Section: Context-dependent Regulation Of Apoptosismentioning

confidence: 99%

Control of apoptosis by Rel/NF-κB transcription factors

1999

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“…17,29,43,44 RICK expression construct was a generous gift from Dr. G Nunez (University of Michigan, Ann Arbor, MI, USA). Kinase inactive mutant of IKK-a were kindly provided by Dr WC Greene (University of California, San Francisco, CA, USA).…”

Section: Origin and Construction Of Expression And Reporter Plasmidsmentioning

confidence: 99%

Regulation of IL-1β generation by Pseudo-ICE and ICEBERG, two dominant negative caspase recruitment domain proteins

et al. 2001

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We report here the identification and functional characterization of two new human caspase recruitment domain (CARD) molecules, termed Pseudo-interleukin-1b converting enzyme (ICE) and ICEBERG. Both proteins share a high degree of homology, reaching 92% and 53% identity, respectively, to the prodomain of caspase-1/ICE. Interestingly, both Pseudo-ICE and ICEBERG are mapped to chromosome 11q22 that bears caspases-1, -4-and -5 genes, all involved in cytokine production rather than in apoptosis. We demonstrate that Pseudo-ICE and ICEBERG interact physically with caspase-1 and block, in a monocytic cell line, the interferon-g and lipopolysaccharide-induced secretion of interleukin-1b which is a well-known consequence of caspase-1 activation. Moreover, Pseudo-ICE, but not ICEBERG, interacts with the CARD-containing kinase RICK/RIP2/CARDIAK and activates NF-kB. Our data suggest that Pseudo-ICE and ICEBERG are intracellular regulators of caspase-1 activation and could play a role in the regulation of IL-1b secretion and NF-kB activation during the pro-inflammatory cytokine response. Cell Death and Differentiation (2001) 8, 649 ± 657.

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CLAP, a Novel Caspase Recruitment Domain-containing Protein in the Tumor Necrosis Factor Receptor Pathway, Regulates NF-κB Activation and Apoptosis

Cited by 107 publications

References 65 publications

Bcl10 and MALT1, Independent Targets of Chromosomal Translocation in MALT Lymphoma, Cooperate in a Novel NF-κB Signaling Pathway

Bcl10 and MALT1, Independent Targets of Chromosomal Translocation in MALT Lymphoma, Cooperate in a Novel NF-κB Signaling Pathway

Control of apoptosis by Rel/NF-κB transcription factors

Regulation of IL-1β generation by Pseudo-ICE and ICEBERG, two dominant negative caspase recruitment domain proteins

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