| First Author | Staal J | Year | 2011 |
| Journal | EMBO J | Volume | 30 |
| Issue | 9 | Pages | 1742-52 |
| PubMed ID | 21448133 | Mgi Jnum | J:171982 |
| Mgi Id | MGI:5002737 | Doi | 10.1038/emboj.2011.85 |
| Citation | Staal J, et al. (2011) T-cell receptor-induced JNK activation requires proteolytic inactivation of CYLD by MALT1. EMBO J 30(9):1742-52 |
| abstractText | The paracaspase mucosa-associated lymphoid tissue 1 (MALT1) is central to lymphocyte activation and lymphomagenesis. MALT1 mediates antigen receptor signalling to NF-kappaB by acting as a scaffold protein. Furthermore, MALT1 has proteolytic activity that contributes to optimal NF-kappaB activation by cleaving the NF-kappaB 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. |
