| Literature DB >> 11090634 |
A G Uren1, K O'Rourke, L A Aravind, M T Pisabarro, S Seshagiri, E V Koonin, V M Dixit.
Abstract
Caspases are cysteine proteases essential to apoptosis. We have identified two families of caspase-like proteins, Paracaspases (found in metazoans and Dictyostelium) and metacaspases (found in plants, fungi, and protozoa). Metazoan paracaspase prodomains contain a death domain and immunoglobulin domains. Several plant metacaspase prodomains contain zinc finger motifs resembling those in the plant hypersensitive response/cell death protein Isd-1. The human paracaspase prodomain binds Bcl10, a protein involved in the t(1;14)(p22;q32) translocation of mucosa-associated lymphoid tissue (MALT) lymphoma. Another MALT lymphoma translocation, t(11;18)(q21;q21), fuses the IAP-2 gene to the MLT1/MALT1 locus, which encodes the human paracaspase. We find that this fusion activates NF-kappaB and that the caspase domain is required for this function, since mutation of the conserved catalytic cysteine attenuates NF-kappaB activation.Entities:
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Year: 2000 PMID: 11090634 DOI: 10.1016/s1097-2765(00)00094-0
Source DB: PubMed Journal: Mol Cell ISSN: 1097-2765 Impact factor: 17.970