Human CARD12 Is a Novel CED4/Apaf-1 Family Member That Induces Apoptosis

Bj, Geddes; Wang, L; Wj, Huang; Lavellee, M; Ga, Manji; Brown, Melissa Shani; Jurman, Mark E.; Cao, Jinxuan; Morgenstern, Jay P.; Merriam, Sarah; Glucksmann, MA; DiStefano, PS; Bertin, John

doi:10.1006/bbrc.2001.4928

Cited by 103 publications

(78 citation statements)

References 27 publications

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“…The nucleotidebinding oligomerization domain (NOD) proteins act as cytosolic regulators of inflammation and apoptosis ( Figure 1B; reviewed in . NOD1 and NOD2 activate the canonical NF-kB pathway in a RICK-dependent manner (Bertin et al, 1999;Geddes et al, 2001;Ogura et al, 2001;Kobayashi et al, 2002). NOD1 and IPAF activate caspase-1 to form an 'inflammasome' required for cleavage of IL-1b during the innate immune response (Poyet et al, 2001;Grenier et al, 2002;Martinon et al, 2002;Wang et al, 2002a;Yoo et al, 2002).…”

Section: Anti-and Proapoptotic Roles For Nf-kb In T Cellsmentioning

confidence: 99%

To be, or not to be: NF-κB is the answer – role of Rel/NF-κB in the regulation of apoptosis

et al. 2003

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Section: Anti-and Proapoptotic Roles For Nf-kb In T Cellsmentioning

confidence: 99%

To be, or not to be: NF-κB is the answer – role of Rel/NF-κB in the regulation of apoptosis

et al. 2003

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“…Both proteins consist of two homophilic protein interaction domains with characteristic structure called death domain fold. Actually, the CARD of ASC interacts with the CARD of CARD12 (Geddes et al, 2001) and the PYD of ASC interacts with caspase-8 (Masumoto et al, 2003). Therefore, it is likely that ASC itself is a FADD-like adaptor that recruits caspase-8 to CARD12.…”

Section: Discussionmentioning

confidence: 99%

Mechanism of ASC-mediated apoptosis: Bid-dependent apoptosis in type II cells

et al. 2006

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Apoptosis-associated speck-like protein containing a CARD (ASC) is an adaptor molecule that mediates apoptotic and inflammatory signals, and implicated in tumor suppression. However, the mechanism of ASCmediated apoptosis has not been well elucidated. Here, we investigated the molecular mechanisms of ASC-mediated apoptosis in several cell lines using a caspase recruitment domain 12-Nod2 chimeric protein that transduces the signal from muramyl dipeptide into ASC-mediated apoptosis. Experiments using dominant-negative mutants, small-interfering RNAs and peptide inhibitors for caspases indicated that caspase-8 was generally required for ASC-mediated apoptosis, whereas a requirement for caspase-9 depended on the cell type. In addition, caspaselike apoptosis-regulatory protein (CLARP)/Fas-like inhibitor protein, a natural caspase-8 inhibitor, suppressed ASC-mediated apoptosis, and ClarpÀ/À mouse embryonic fibroblasts were highly sensitive to ASC-mediated apoptosis. Bax-deficient HCT116 cells were resistant to ASC-mediated apoptosis as reported previously, although we failed to observe colocalization of ASC and Bax in cells. Like Fas-ligand-induced apoptosis, the ASC-mediated apoptosis was inhibited by Bcl-2 and/or Bcl-XL in type-II but not type-I cell lines. Bid was cleaved upon ASC activation, and suppression of endogenous Bid expression using small-interfering RNAs in type-II cells reduced the ASC-mediated apoptosis. These results indicate that ASC, like death receptors, mediates two types of apoptosis depending on the cell type, in a manner involving caspase-8.

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“…However, degradation products of the same size were also seen in the presence of caspase inhibitors (results not shown), suggesting that a different protease is responsible. In addition, caspase-1 activation occurs through a so-called induced proximity mechanism 34 via amino-terminal CARD interactions, and only CARD proteins have been identified as procaspase-1 activators, for example, RIP2/RICK/CARDIAK, 39-41 CARD12/CLAN/Ipaf [42][43][44] and Asc. 9,21 Thus, it seems unlikely that a protein without a CARD, such as EBBP, is a caspase-1 activator.…”

Section: Discussionmentioning

confidence: 99%

The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

et al. 2006

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The estrogen-responsive B box protein (EBBP) and Pyrin belong to a family of structurally related proteins. While mutations in the pyrin gene cause an autoinflammatory disease, the biological function of EBBP is unknown. In this study, we identified the proinflammatory cytokine interleukin1b (IL-1b) as an EBBP-binding partner. Furthermore, caspase-1 and NACHT, LRR and Pyrin domain containing protein (NALP) 1, two components of the recently identified inflammasome, a platform for the activation of caspase-1, also interact with EBBP. These proteins bind to the RFP domain of EBBP, suggesting that this domain of so far unknown function is an important protein-binding domain. EBBP was secreted in a caspase-1-dependent manner from cultured cells, and its secretion was enhanced by IL-1b. Vice versa, endogenous and overerexpressed EBBP increased IL-1b secretion. These results provide evidence for a role of EBBP in innate immunity by enhancing the alternative secretion pathway of IL-1b.

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Human CARD12 Is a Novel CED4/Apaf-1 Family Member That Induces Apoptosis

Cited by 103 publications

References 27 publications

To be, or not to be: NF-κB is the answer – role of Rel/NF-κB in the regulation of apoptosis

To be, or not to be: NF-κB is the answer – role of Rel/NF-κB in the regulation of apoptosis

Mechanism of ASC-mediated apoptosis: Bid-dependent apoptosis in type II cells

The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

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