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TitleMolecular architecture and regulation of BCL10-MALT1 filaments.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 4041, Year 2018
Publish dateOct 2, 2018
AuthorsFlorian Schlauderer / Thomas Seeholzer / Ambroise Desfosses / Torben Gehring / Mike Strauss / Karl-Peter Hopfner / Irina Gutsche / Daniel Krappmann / Katja Lammens /
PubMed AbstractThe 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 ...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.
External linksNat Commun / PubMed:30279415 / PubMed Central
MethodsEM (helical sym.)
Resolution4.9 Å
Structure data

0013

6gk2

EMDB-0013, PDB-6gk2:
Helical reconstruction of BCL10 CARD and MALT1 DEATH DOMAIN complex
Method: EM (helical sym.) / Resolution: 4.9 Å

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / BCL10 / MALT1 / CBM complex / helical reconstruction / cancer / autoimmune disease

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