Evidence map›Paper›PMID 24074955›Full record

ArticleMolecular cell2013

Structural architecture of the CARMA1/Bcl10/MALT1 signalosome: nucleation-induced filamentous assembly.

Qi Qiao, Chenghua Yang, Chao Zheng, Lorena Fontán, Liron David, Xiong Yu, Clay Bracken, Monica Rosen, Ari Melnick, Edward H Egelman and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
6.4field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

104 citing papers in PubMed, 173 citations in OpenAlex.

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  18. MALT1 substrate cleavage: what is it good for?Frontiers in immunology · 2024
    Review
  19. Identification of Tensin-3 as a MALT1 substrate that controls B cell adhesion and lymphoma dissemination.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Review

44 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 1 country.

Qi QiaoDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
Chenghua Yang
Chao Zheng
Lorena Fontán
Liron David
Xiong Yu
Clay Bracken
Monica Rosen
Ari Melnick
Edward H Egelman
Hao Wu
Cornell University · USBoston Children's Hospital · USUniversity of Virginia · US

Funding

Structural Studies of TNF Receptor Associated Factors (TRAFs)R01AI045937 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI WU, HAO · 1999 to 2016
$5.9M
Methods for the Analysis of Helical Macromolecular ComplexesR01EB001567 · NIBIB · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI EGELMAN, EDWARD H. · 2003 to 2014
$3.6M
Molecular elucidation of the CBM complex in NF-kappaB activation by antigen recepR01AI089882 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI WU, HAO · 2010 to 2014
$1.9M
NIAID NIH HHS R01 AI045937NIAID NIH HHS R01 AI089882NIAID NIH HHS R01AI089882NIBIB NIH HHS R01 EB001567NIBIB NIH HHS R01EB001567
6 · The paper itself

Abstract

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.

Indexed as

Adaptor Proteins, Signal TransducingB-Cell CLL-Lymphoma 10 ProteinBinding SitesCARD Signaling Adaptor ProteinsCaspasesCrystallography, X-RayGene Expression RegulationGuanylate CyclaseHumansJurkat CellsMucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 ProteinMultiprotein ComplexesNeoplasm ProteinsNF-kappa BProtein BindingProtein Structure, SecondaryAdaptor Proteins, Signal TransducingB-Cell CLL-Lymphoma 10 ProteinBCL10 protein, humanCARD11 protein, humanCARD Signaling Adaptor ProteinsCaspasesGuanylate CyclaseMALT1 protein, humanMucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 ProteinMultiprotein ComplexesNeoplasm ProteinsNF-kappa B

Identifiers

PMID24074955
PMCPMC3929958
OpenAlexW2086569749

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.