ArticleThe Biochemical journal2012
Mechanism and specificity of the human paracaspase MALT1.
Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
44 citing papers in PubMed, 89 citations in OpenAlex.
- Loop dynamics govern MALT1 activation revealed by integrative AlphaFold, MD, and NMR analysis.Scientific reports · 2026Article
- Insight into Malt1 activation mechanism through synergetic approach of AlphaFold, MD Simulation and NMR dynamic analyses.bioRxiv : the preprint server for biology · 2025Article
- Insights into mechanisms of MALT1 allostery from NMR and AlphaFold dynamic analyses.Communications biology · 2024Article
- Thermoprotection by a cell membrane-localized metacaspase in a green alga.The Plant cell · 2024Article
- MALT1 substrate cleavage: what is it good for?Frontiers in immunology · 2024Review
- Identification of Tensin-3 as a MALT1 substrate that controls B cell adhesion and lymphoma dissemination.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cotargeting of BTK and MALT1 overcomes resistance to BTK inhibitors in mantle cell lymphoma.The Journal of clinical investigation · 2023Article
- Assignment of IVL-Methyl side chain of the ligand-free monomeric human MALT1 paracaspase-IgLBiomolecular NMR assignments · 2022Article
- Integrating knowledge of protein sequence with protein function for the prediction and validation of new MALT1 substrates.Computational and structural biotechnology journal · 2022Article
- CARD10 cleavage by MALT1 restricts lung carcinoma growth in vivo.Oncogenesis · 2021Article
- Structural Determinants of Substrate Specificity of SplF Protease fromInternational journal of molecular sciences · 2021Article
- Insights Into the Phylogenetic Distribution, Diversity, Structural Attributes, and Substrate Specificity of Putative Cyanobacterial Orthocaspases.Frontiers in microbiology · 2021Article
- The tale of caspase homologues and their evolutionary outlook: deciphering programmed cell death in cyanobacteria.Journal of experimental botany · 2020Article
- MALT-1 mediates IL-17 neural signaling to regulate C. elegans behavior, immunity and longevity.Nature communications · 2020Article
- Classification and Nomenclature of Metacaspases and Paracaspases: No More Confusion with Caspases.Molecular cell · 2020Article
- Allosteric activation of MALT1 by its ubiquitin-binding Ig3 domain.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Peptide-based covalent inhibitors of MALT1 paracaspase.Bioorganic & medicinal chemistry letters · 2019Article
- Metacaspases: Potential Drug Target Against Protozoan Parasites.Frontiers in pharmacology · 2019Review
- Phylogenetic Distribution and Diversity of Bacterial Pseudo-Orthocaspases Underline Their Putative Role in Photosynthesis.Frontiers in plant science · 2019Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
The paracaspase domain of MALT1 (mucosa-associated lymphoid tissue lymphoma translocation protein 1) is a component of a gene translocation fused to the N-terminal domains of the cellular inhibitor of apoptosis protein 2. The paracaspase itself, commonly known as MALT1, participates in the NF-κB (nuclear factor κB) pathway, probably by driving survival signals downstream of the B-cell antigen receptor through MALT1 proteolytic activity. We have developed methods for the expression and purification of recombinant full-length MALT1 and its constituent catalytic domain alone. Both are activated by dimerization without cleavage, with a similar dimerization barrier to the distantly related cousins, the apical caspases. By using positional-scanning peptidyl substrate libraries we demonstrate that the activity and specificity of full-length MALT1 is recapitulated by the catalytic domain alone, showing a stringent requirement for cleaving after arginine, and with striking peptide length constraints for efficient hydrolysis. Rates of cleavage (kcat/Km values) of optimal peptidyl substrates are in the same order (10(3)-10(4) M(-1)·s(-1)) as for a putative target protein CYLD. Thus MALT1 has many similarities to caspase 8, even cleaving the putative target protein CYLD with comparable efficiencies, but with diametrically opposite primary substrate specificity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.