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- Title
The proteolytic activity of the paracaspase MALT1 is key in T cell activation.
- Authors
Rebeaud, Fabien; Hailfinger, Stephan; Posevitz-Fejfar, Anita; Tapernoux, Myriam; Moser, Roger; Rueda, Daniel; Gaide, Olivier; Guzzardi, Montserrat; Iancu, Emanuela M; Rufer, Nathalie; Fasel, Nicolas; Thome, Margot
- 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.
- Publication
Nature immunology, 2008, Vol 9, Issue 3, p272
- ISSN
1529-2916
- Publication type
Journal Article
- DOI
10.1038/ni1568