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Caspases leave the beaten track: caspase-mediated activation of NF-B

Unit of Molecular Signaling and Cell Death, Department for Molecular Biomedical Research, Flanders Interuniversity Institute for Biotechnology (VIB), Ghent University, B-9052 Ghent, Belgium

Correspondence to Peter Vandenabeele: peter.vandenabeele{at}dmbr.ugent.be

The proteolytic activity of the cysteinyl aspartate–specific proteases, named caspases, mainly connotes their central role in apoptosis and inflammation. In this review we report on recent data on the role of caspases in the activation of nuclear factor B (NF-B), a transcription factor that fulfils a central role in innate and adaptive immunity, in cellular stress responses and in the induction of anti-apoptotic factors. Two different mechanisms by which caspases activate the NF-B pathway are discussed.

Abbreviations used in this paper: CARD, caspase recruitment domain; DISC, death-inducing signaling complex; FADD, Fas-associated death domain-containing protein; IKK, IB kinase; IL, interleukin; LPS, lipopolysaccharide; NF-B, nuclear factor B; NLR, NACHT-LRR; PARP, poly(ADP-ribose)polymerase; PIDD, p53-induced death domain protein, RIP, receptor interacting protein; TcR, T-cell receptor; TLR, toll-like receptor; TRAF, tumor necrosis factor-receptor associated factor.

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