PUBLICATION
Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma
- Authors
- Uren, A.G., O'Rourke, K., Aravind, L.A., Pisabarro, M.T., Seshagiri, S., Koonin, E.V., and Dixit, V.M.
- ID
- ZDB-PUB-020806-3
- Date
- 2000
- Source
- Molecular Cell 6(4): 961-967 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Caspases/chemistry
- Caspases/genetics*
- Chromosome Mapping
- Chromosomes, Human, Pair 1
- Chromosomes, Human, Pair 14
- Cloning, Molecular
- Dictyostelium/enzymology
- Dictyostelium/genetics
- Humans
- Lymphoma, B-Cell, Marginal Zone/enzymology*
- Lymphoma, B-Cell, Marginal Zone/genetics*
- Molecular Sequence Data
- Recombinant Proteins/biosynthesis
- Recombinant Proteins/chemistry
- Sequence Alignment
- Sequence Homology, Amino Acid
- Species Specificity
- Transfection
- Translocation, Genetic
- Zinc Fingers
- PubMed
- 11090634 Full text @ Mol. Cell
Citation
Uren, A.G., O'Rourke, K., Aravind, L.A., Pisabarro, M.T., Seshagiri, S., Koonin, E.V., and Dixit, V.M. (2000) Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma. Molecular Cell. 6(4):961-967.
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping