%0 Journal Article %T TAK1 lessens the Activity of the Paracaspase MALT1 during T cell Receptor Signaling %+ Signaling in Oncogenesis, Angiogenesis and Permeability (CRCINA-ÉQUIPE 15) %+ L’Héma-NexT [UNIV Nantes] (i-Site NexT) %+ Microenvironnement des niches tumorales (CNRS GDR 3697 Micronit ) %+ Institut de Cancérologie de l'Ouest [Angers/Nantes] (UNICANCER/ICO) %A Alves Nicolau, Carolina %A Gavard, Julie %A Bidère, Nicolas %Z This research was funded by an International Program for Scientific Cooperation (PICS, CNRS), Fondation ARC contre le Cancer (JG, NB), Ligue nationale contre le cancer comités de Loire-Atlantique, Maine et Loire,Vendée (JG, NB), Région Pays de la Loire et Nantes Métropole under Connect Talent Grant (JG), the National Research Agency under the Programme d’Investissements d’Avenir (ANR-16-IDEX-0007), and by the SIRIC ILIAD (INCa-DGOS-Inserm_12558). CAN holds a postdoctoral fellowship from Fondation de France. Team projects are funded by Equipe Labellisée Fondation pour la Recherche Médicale (FRM DEQ20180339184). %< avec comité de lecture %@ 0008-8749 %J Cellular Immunology %I Elsevier %P 104115 %8 2020-04-28 %D 2020 %R 10.1016/j.cellimm.2020.104115 %K NF-κB %K Signaling %K Lymphocyte %K TAK1 %K MALT1 %K CBM complex %Z Life Sciences [q-bio]/CancerJournal articles %X The CARMA1-BCL10-MALT1 (CBM) complex couples antigen receptors to the activation of Nuclear Factor κB (NF-κB) transcription factors in T/B lymphocytes. Within this signalosome, the MALT1 paracaspase serves dual roles: it is a crucial adaptor for signal transduction to NF-κB signaling, and a protease that shapes NF-κB activity and lymphocyte activation. Although a subtle choreography of ubiquitination and phosphorylation orchestrate the CBM, how precisely this complex and MALT1 enzyme are regulated continue to be elucidated. Here, we report that the chemical inhibition or the siRNA-based silencing of transforming growth factor beta-activated kinase 1 (TAK1), a known partner of the CBM complex required for NF-κB activation, enhanced the processing of MALT1 substrates. We further show that the assembly of the CBM as well as the ubiquitination of MALT1 was augmented when TAK1 was inhibited. Thus, TAK1 may initiate a negative feedback loop to finely tune the CBM complex activity. %G English %2 https://inserm.hal.science/inserm-02558368/document %2 https://inserm.hal.science/inserm-02558368/file/Gavard2020Eq15.pdf %L inserm-02558368 %U https://inserm.hal.science/inserm-02558368 %~ INSERM %~ UNIV-NANTES %~ CNRS %~ UNIV-ANGERS %~ LORIA2 %~ CRCINA %~ ANR %~ NANTES-UNIVERSITE %~ UNIV-NANTES-AV2022 %~ FRM