TAK1 lessens the Activity of the Paracaspase MALT1 during T cell Receptor Signaling
Autor: | Nicolas Bidère, Julie Gavard, Carolina Alves Nicolau |
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Přispěvatelé: | Signaling in Oncogenesis, Angiogenesis and Permeability (CRCINA-ÉQUIPE 15), Centre de Recherche en Cancérologie et Immunologie Nantes-Angers (CRCINA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN)-Centre hospitalier universitaire de Nantes (CHU Nantes)-Centre National de la Recherche Scientifique (CNRS)-Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN)-Centre hospitalier universitaire de Nantes (CHU Nantes)-Centre National de la Recherche Scientifique (CNRS)-Université d'Angers (UA), L’Héma-NexT [UNIV Nantes] (i-Site NexT), Université de Nantes (UN), Microenvironnement des niches tumorales [UNIV Tours] (CNRS GDR 3697 MicroNiT), Université de Tours-Centre National de la Recherche Scientifique (CNRS), Institut de Cancérologie de l'Ouest [Angers/Nantes] (UNICANCER/ICO), UNICANCER, 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)., Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS), Université d'Angers (UA)-Université de Nantes (UN)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre hospitalier universitaire de Nantes (CHU Nantes)-Université d'Angers (UA)-Université de Nantes (UN)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre hospitalier universitaire de Nantes (CHU Nantes), Microenvironnement des niches tumorales (CNRS GDR 3697 Micronit ), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Bernardo, Elizabeth |
Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
0301 basic medicine
TAK1 Immunology Receptors Antigen T-Cell [SDV.CAN]Life Sciences [q-bio]/Cancer Biology Lymphocyte Activation NF-κB Jurkat Cells 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine [SDV.CAN] Life Sciences [q-bio]/Cancer CBM complex Humans Gene silencing Phosphorylation Transcription factor Adaptor Proteins Signal Transducing B-Lymphocytes MALT1 NF-kappa B Paracaspase MAP Kinase Kinase Kinases Signaling Neoplasm Proteins Cell biology 030104 developmental biology chemistry Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein Multiprotein Complexes Lymphocyte Signal transduction Signal Transduction Transcription Factors 030215 immunology |
Zdroj: | Cellular Immunology Cellular Immunology, Elsevier, 2020, pp.104115. ⟨10.1016/j.cellimm.2020.104115⟩ Cellular Immunology, 2020, pp.104115. ⟨10.1016/j.cellimm.2020.104115⟩ |
ISSN: | 0008-8749 1090-2163 |
Popis: | International audience; 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. |
Databáze: | OpenAIRE |
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