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Molecular architecture and regulation of BCL10-MALT1 filaments

Schlauderer, Florian ; Seeholzer, Thomas ; Desfosses, Ambroise ; Gehring, Torben ; Strauss, Mike ; Hopfner, Karl-Peter ; Gutsche, Irina ; Krappmann, Daniel ; Lammens, Katja

Nature communications, 2018-10, Vol.9 (1), p.4041-12, Article 4041 [Periódico revisado por pares]

England: Nature Publishing Group

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Título:
Molecular architecture and regulation of BCL10-MALT1 filaments
Autor: Schlauderer, Florian ; Seeholzer, Thomas ; Desfosses, Ambroise ; Gehring, Torben ; Strauss, Mike ; Hopfner, Karl-Peter ; Gutsche, Irina ; Krappmann, Daniel ; Lammens, Katja
Assuntos: Adaptive immunity ; Architecture ; Assembly ; B-Cell CLL-Lymphoma 10 Protein - chemistry ; B-Cell CLL-Lymphoma 10 Protein - metabolism ; B-Cell CLL-Lymphoma 10 Protein - ultrastructure ; Bcl-10 protein ; Biochemistry, Molecular Biology ; CARD Signaling Adaptor Proteins - metabolism ; Caspase ; CD4 antigen ; Cryoelectron Microscopy ; Domains ; Filaments ; Guanylate Cyclase - metabolism ; Immune response ; Immune system ; Immunoglobulins ; Interfaces ; Kinases ; Life Sciences ; Lymphocyte Activation ; Lymphocytes ; Lymphocytes T ; Lymphoma ; Models, Chemical ; Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein - chemistry ; Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein - metabolism ; Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein - ultrastructure ; Mutagenesis ; Mutation ; NF-κB protein ; Paracaspases ; Protein Conformation ; Proteins ; Signaling ; Structural Biology ; Substrates
É parte de: Nature communications, 2018-10, Vol.9 (1), p.4041-12, Article 4041
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descrição: The CARD11-BCL10-MALT1 (CBM) complex triggers the adaptive immune response in lymphocytes and lymphoma cells. CARD11/CARMA1 acts as a molecular seed inducing BCL10 filaments, but the integration of MALT1 and the assembly of a functional CBM complex has remained elusive. Using cryo-EM we solved the helical structure of the BCL10-MALT1 filament. The structural model of the filament core solved at 4.9 Å resolution identified the interface between the N-terminal MALT1 DD and the BCL10 caspase recruitment domain. The C-terminal MALT1 Ig and paracaspase domains protrude from this core to orchestrate binding of mediators and substrates at the filament periphery. Mutagenesis studies support the importance of the identified BCL10-MALT1 interface for CBM complex assembly, MALT1 protease activation and NF-κB signaling in Jurkat and primary CD4 T-cells. Collectively, we present a model for the assembly and architecture of the CBM signaling complex and how it functions as a signaling hub in T-lymphocytes.
Editor: England: Nature Publishing Group
Idioma: Inglês

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Molecular architecture and regulation of BCL10-MALT1 filaments

Schlauderer, Florian ; Seeholzer, Thomas ; Desfosses, Ambroise ; Gehring, Torben ; Strauss, Mike ; Hopfner, Karl-Peter ; Gutsche, Irina ; Krappmann, Daniel ; Lammens, Katja

England: Nature Publishing Group

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