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

Rebeaud, Fabien
Hailfinger, Stephan
Posevitz-Fejfar, Anita
Moser, Roger
Rueda, Daniel
Guzzardi, Montserrat
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Published in Nature immunology. 2008, vol. 9, no. 3, p. 272-81
Abstract 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.
Keywords Adaptor Proteins, Signal Transducing/metabolismCaspases/physiologyCell LineElectrophoresis, Gel, Two-DimensionalHumansJurkat CellsLymphocyte Activation/immunologyNF-kappa B/metabolismNeoplasm Proteins/physiologyPeptide Hydrolases/metabolismProtein Isoforms/metabolismT-Lymphocytes/immunology
PMID: 18264101
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Research group Voies d'activation de l'immunité innée au niveau de la peau (156)
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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. 272-81. https://archive-ouverte.unige.ch/unige:2017

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Deposited on : 2009-06-12

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