Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma.
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.
Mesh Terms:
Amino Acid Sequence, Animals, Caspases, Chromosome Mapping, Chromosomes, Human, Pair 1, Chromosomes, Human, Pair 14, Cloning, Molecular, Dictyostelium, Humans, Lymphoma, B-Cell, Marginal Zone, Molecular Sequence Data, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Species Specificity, Transfection, Translocation, Genetic, Zinc Fingers
Amino Acid Sequence, Animals, Caspases, Chromosome Mapping, Chromosomes, Human, Pair 1, Chromosomes, Human, Pair 14, Cloning, Molecular, Dictyostelium, Humans, Lymphoma, B-Cell, Marginal Zone, Molecular Sequence Data, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Species Specificity, Transfection, Translocation, Genetic, Zinc Fingers
Mol. Cell
Date: Oct. 01, 2000
PubMed ID: 11090634
View in: Pubmed Google Scholar
Download Curated Data For This Publication
11770
Switch View:
- Interactions 3