Identification of Paracaspases and Metacaspases Two Ancient Families of Caspase-like Proteins, One of which Plays a Key Role in MALT Lymphoma
| Autor: | A G, Uren, K, O'Rourke, L A, Aravind, M T, Pisabarro, S, Seshagiri, E V, Koonin, V M, Dixit |
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| Rok vydání: | 2000 |
| Předmět: |
Molecular Sequence Data
Immunoglobulin domain Transfection Translocation Genetic Species Specificity Animals Humans Dictyostelium Amino Acid Sequence Cloning Molecular Molecular Biology Caspase Death domain Chromosomes Human Pair 14 Zinc finger Sequence Homology Amino Acid biology Chromosome Mapping Zinc Fingers Lymphoma B-Cell Marginal Zone Cell Biology Paracaspase Recombinant Proteins Metacaspase BCL10 MALT1 Biochemistry Chromosomes Human Pair 1 Caspases biology.protein Sequence Alignment |
| Zdroj: | Molecular Cell. 6:961-967 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/s1097-2765(00)00094-0 |
| Popis: | 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 lsd-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-κB and that the caspase domain is required for this function, since mutation of the conserved catalytic cysteine attenuates NF-κB activation. |
| Databáze: | OpenAIRE |
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