Activation of Caspase-1 in the Nucleus Requires Nuclear Translocation of Pro-caspase-1 Mediated by Its Prodomain

Mao, Pei-Lin; Jiang, Yalin; Wee, Boon Yu; Porter, Alan G.

doi:10.1074/jbc.273.37.23621

Cited by 76 publications

(59 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…40 Upon treatment of HeLa cells with TNF, procaspase-1 localizes to the nucleus in a prodomain dependent manner. 41 Recently, caspase-9 has also been shown to translocate from the mitochondria to nucleus upon induction of apoptosis. 42 Apoptosis inducing factor (AIF), a flavoprotein that is released from mitochondria during apoptosis, functions by mediating changes in the nucleus 43 and is thus likely to be imported into nucleus.…”

Section: Discussionmentioning

confidence: 99%

Subcellular localization and CARD-dependent oligomerization of the death adaptor RAIDD

2000

View full text Add to dashboard Cite

RAIDD, a caspase recruitment domain (CARD) containing molecule, interacts with procaspase-2 in a CARD-dependent manner. This interaction has been suggested to mediate the recruitment of caspase-2 to the tumour necrosis factor receptor 1 (TNFR1). In this paper we have studied the subcellular localization of RAIDD and its interaction with caspase-2. We demonstrate that endogenous RAIDD is mostly localized in the cytoplasm and to some extent in the nucleus. RAIDD localization is not affected by TNF-treatment of HeLa cells, but in cells ectopically expressing caspase-2, a fraction of RAIDD is recruited to the nucleus. In transfected cells, coexpression of RAIDD and caspase-2 leads to CARDdependent colocalization of the two proteins to discrete subcellular structures. We further show that overexpression of the RAIDD-CARD results in the formation of filamentous structures due to CARD-mediated oligomerization. These structures were similar to death effector filaments (DEFs) formed by FADD and FLICE death effector domains (DEDs), and partially colocalized with DEFs. Our results suggest that similar to the DED, the RAIDD-CARD has the ability to form higher order complexes, believed to be important in apoptotic execution. We also present evidence that RAIDD-CARD oligomerization may be regulated by intramolecular folding of the RAIDD molecule. Cell Death and Differentiation (2000) 7, 155 ± 165.

show abstract

Section: Discussionmentioning

confidence: 99%

Subcellular localization and CARD-dependent oligomerization of the death adaptor RAIDD

2000

View full text Add to dashboard Cite

show abstract

“…65 Procaspase-1 was also reported to bear an NLS; these results, however, were based solely on subcellular fractionation experiments. 83 The absence of canonical transport sequences in the caspases' primary structures however does not rule out the possibility that they may enter the nucleus by alternative, NLSindependent active transport pathways, as reported, for example, for b-catenin or ERK2. 84,85 In fact, Kamada et al recently proposed that active caspase-3 is translocated into the nucleus of apoptotic cells by association with a yet unknown substrate molecule.…”

Section: Poly-adp-ribose (Par)mentioning

confidence: 99%

Nucleocytoplasmic transport in apoptosis

Ferrando‐May

2005

Cell Death Differ

View full text Add to dashboard Cite

The apoptotic demolition of the nucleus is accomplished by diverse proapoptotic factors, most of which are activated in the cytoplasm and gain access to the nucleoplasm during the cell death process. The nucleus is also the main target for genotoxic insult, a potent apoptotic trigger. Signals generated in the nucleus by DNA damage have to propagate to all cellular compartments to ensure the coordinated execution of cell demise. The nucleocytoplasmic shuttling of signalling and execution factors is thus an integral part of the apoptotic programme. Several proteins implicated in apoptotic cell death have been shown to migrate in and out of the nucleus following apoptosis induction. This review summarises the current knowledge on nucleocytoplasmic trafficking of apoptosis-relevant proteins. The effects of apoptosis induction on the nucleocytoplasmic transport machinery are also discussed. Finally, a potential role of nuclear transport as a critical control point of the apoptotic signal cascade is proposed.

show abstract

“…26 According to Mao et al, 26 a lysine/arginine rich segment at residues 4 ± 11 (KVLKEKRK) that resembles a nuclear localization signal, would be responsible for caspase-1 prodomain nuclear translocation. Despite of the highly conserved sequence, especially at residues 4 ± 11, of Pseudo-ICE, this protein did not induce significant apoptosis when overexpressed in MCF-7 Fas cells and did not affect tumor necrosis factor (TNF)-a-induced apoptosis ( Figure 5).…”

Section: Pseudo-ice and Iceberg Do Not Induce Apoptosis In Mcf-7 Fas mentioning

confidence: 99%

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

et al. 2001

View full text Add to dashboard Cite

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.

show abstract

Activation of Caspase-1 in the Nucleus Requires Nuclear Translocation of Pro-caspase-1 Mediated by Its Prodomain

Cited by 76 publications

References 26 publications

Subcellular localization and CARD-dependent oligomerization of the death adaptor RAIDD

Subcellular localization and CARD-dependent oligomerization of the death adaptor RAIDD

Nucleocytoplasmic transport in apoptosis

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

Contact Info

Product

Resources

About