Scientific article

The proteolytic activity of the paracaspase MALT1 is key in T cell activation

Published inNature immunology, vol. 9, no. 3, p. 272-281
Publication date2008

The paracaspase MALT1 is pivotal in antigen receptor-mediated lymphocyte activation and lymphomagenesis. MALT1 contains a caspase-like domain, but it is unknown whether this domain is proteolytically active. Here we report that MALT1 had arginine-directed proteolytic activity that was activated after T cell stimulation, and we identify the signaling protein Bcl-10 as a MALT1 substrate. Processing of Bcl-10 after Arg228 was required for T cell receptor-induced cell adhesion to fibronectin. In contrast, MALT1 activity but not Bcl-10 cleavage was essential for optimal activation of transcription factor NF-kappaB and production of interleukin 2. Thus, the proteolytic activity of MALT1 is central to T cell activation, which suggests a possible target for the development of immunomodulatory or anticancer drugs.

  • Adaptor Proteins, Signal Transducing/metabolism
  • Caspases/physiology
  • Cell Line
  • Electrophoresis, Gel, Two-Dimensional
  • Humans
  • Jurkat Cells
  • Lymphocyte Activation/immunology
  • NF-kappa B/metabolism
  • Neoplasm Proteins/physiology
  • Peptide Hydrolases/metabolism
  • Protein Isoforms/metabolism
  • T-Lymphocytes/immunology
Citation (ISO format)
REBEAUD, Fabien et al. The proteolytic activity of the paracaspase MALT1 is key in T cell activation. In: Nature immunology, 2008, vol. 9, n° 3, p. 272–281. doi: 10.1038/ni1568
Main files (1)
Article (Accepted version)
ISSN of the journal1529-2916

Technical informations

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