Journal
EMBO JOURNAL
Volume 30, Issue 9, Pages 1742-1752Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/emboj.2011.85
Keywords
AP-1; cytokine; MAP kinase; signal transduction; ubiquitination
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Funding
- Interuniversity Attraction Poles program [IAP6/18)]
- FWO [G.0089.10]
- Belgian Foundation against Cancer
- 'Strategic Basis Research program' of the IWT
- Centrum voor Gezwelziekten
- Concerted Research Actions (GOA) [01G06B6]
- 'Group-ID MRP' initiative of the Ghent University
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The paracaspase mucosa-associated lymphoid tissue 1 (MALT1) is central to lymphocyte activation and lymphomagenesis. MALT1 mediates antigen receptor signalling to NF-kappa B by acting as a scaffold protein. Furthermore, MALT1 has proteolytic activity that contributes to optimal NF-kappa B activation by cleaving the NF-kappa B inhibitor A20. Whether MALT1 protease activity is involved in other signalling pathways, and the identity of the relevant substrates, is unknown. Here, we show that T-cell receptors (TCR) activation, as well as overexpression of the oncogenic API2-MALT1 fusion protein, results in proteolytic inactivation of CYLD by MALT1, which is specifically required for c-jun N-terminal kinase (JNK) activation and the inducible expression of a subset of genes. These results indicate a novel role for MALT1 proteolytic activity in TCR-induced JNK activation and reveal CYLD cleavage as the underlying mechanism. The EMBO Journal (2011) 30, 1742-1752. doi:10.1038/emboj.2011.85; Published online 29 March 2011
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