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TitleStructural architecture of the CARMA1/Bcl10/MALT1 signalosome: nucleation-induced filamentous assembly.
Journal, issue, pagesMol Cell, Vol. 51, Issue 6, Page 766-779, Year 2013
Publish dateSep 26, 2013
AuthorsQi Qiao / Chenghua Yang / Chao Zheng / Lorena Fontán / Liron David / Xiong Yu / Clay Bracken / Monica Rosen / Ari Melnick / Edward H Egelman / Hao Wu /
PubMed AbstractThe CARMA1/Bcl10/MALT1 (CBM) signalosome mediates antigen receptor-induced NF-κB signaling to regulate multiple lymphocyte functions. While CARMA1 and Bcl10 contain caspase recruitment domains ...The CARMA1/Bcl10/MALT1 (CBM) signalosome mediates antigen receptor-induced NF-κB signaling to regulate multiple lymphocyte functions. While CARMA1 and Bcl10 contain caspase recruitment domains (CARDs), MALT1 is a paracaspase with structural similarity to caspases. Here we show that the reconstituted CBM signalosome is a helical filamentous assembly in which substoichiometric CARMA1 nucleates Bcl10 filaments. Bcl10 filament formation is a highly cooperative process whose threshold is sensitized by oligomerized CARMA1 upon receptor activation. In cells, both cotransfected CARMA1/Bcl10 complex and the endogenous CBM signalosome are filamentous morphologically. Combining crystallography, nuclear magnetic resonance, and electron microscopy, we reveal the structure of the Bcl10 CARD filament and the mode of interaction between CARMA1 and Bcl10. Structure-guided mutagenesis confirmed the observed interfaces in Bcl10 filament assembly and MALT1 activation in vitro and NF-κB activation in cells. These data support a paradigm of nucleation-induced signal transduction with threshold response due to cooperativity and signal amplification by polymerization.
External linksMol Cell / PubMed:24074955 / PubMed Central
MethodsEM (helical sym.) / NMR (solution) / X-ray diffraction
Resolution1.792 - 20.0 Å
Structure data

EMDB-5729:
Bcl10 filament
Method: EM (helical sym.) / Resolution: 20.0 Å

PDB-2mb9:
Human Bcl10 CARD
Method: SOLUTION NMR

PDB-4lwd:
Human CARMA1 CARD domain
Method: X-RAY DIFFRACTION / Resolution: 1.792 Å

Chemicals

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / Death domain / APOPTOSIS / Bcl10

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