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

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

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  • 2008-02-12
Published in:
  • Nature immunology. - 2008
Adaptor Proteins, Signal Transducing
B-Cell CLL-Lymphoma 10 Protein
Caspases
Cell Line
Electrophoresis, Gel, Two-Dimensional
Humans
Jurkat Cells
Lymphocyte Activation
Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein
NF-kappa B
Neoplasm Proteins
Peptide Hydrolases
Protein Isoforms
T-Lymphocytes
English 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.
Language
  • English
Open access status
closed
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Persistent URL
https://sonar.ch/global/documents/122792
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