AIP augments CARMA1-BCL10-MALT1 complex formation to facilitate NF-κB signaling upon T cell activation

Schimmack, Gisela; Eitelhuber, Andrea C.; Vincendeau, Michelle; Demski, Katrin; Shinohara, Hisaaki; Kurosaki, Tomohiro; Krappmann, Daniel

doi:10.1186/s12964-014-0049-7

Cited by 21 publications

(14 citation statements)

References 27 publications

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“…For immunoprecipitation studies cells were lysed in co-IP buffer (25 m M 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid pH 7.5, 150 m M NaCl, 0.2% NP-40, 10% glycerol, phosphatase inhibitors 1 m M dithiothreitol, 10 m M sodium fluoride, 8 m M β-glycerophosphate, 300 μ M sodium vanadate and protease inhibitors (Roche, Grenzach, Germany)) followed by antibody incubation as described previously. 52 For disruption of nuclei, cells were additionally passed through a 26-gauge needle. StrepTactin-PD were conducted in co-IP buffer using Strep Tactin-Sepharose (IBA).…”

Section: Methodsmentioning

confidence: 99%

Oncogenic CARMA1 couples NF-κB and β-catenin signaling in diffuse large B-cell lymphomas

et al. 2016

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Constitutive activation of the antiapoptotic nuclear factor-κB (NF-κB) signaling pathway is a hallmark of the activated B-cell-like (ABC) subtype of diffuse large B-cell lymphomas (DLBCL). Recurrent oncogenic mutations are found in the scaffold protein CARMA1 (CARD11) that connects B-cell receptor (BCR) signaling to the canonical NF-κB pathway. We asked how far additional downstream processes are activated and contribute to the oncogenic potential of DLBCL-derived CARMA1 mutants. To this end, we expressed oncogenic CARMA1 in the NF-κB negative DLBCL lymphoma cell line BJAB. By a proteomic approach we identified recruitment of β-catenin and its destruction complex consisting of APC, AXIN1, CK1α and GSK3β to oncogenic CARMA1. Recruitment of the β-catenin destruction complex was independent of CARMA1-BCL10-MALT1 complex formation or constitutive NF-κB activation and promoted the stabilization of β-catenin. The β-catenin destruction complex was also recruited to CARMA1 in ABC DLBCL cell lines, which coincided with elevated β-catenin expression. In line, β-catenin was frequently detected in non-GCB DLBCL biopsies that rely on chronic BCR signaling. Increased β-catenin amounts alone were not sufficient to induce classical WNT target gene signatures, but could augment TCF/LEF-dependent transcriptional activation in response to WNT signaling. In conjunction with NF-κB, β-catenin enhanced expression of immunosuppressive interleukin-10 and suppressed antitumoral CCL3, indicating that β-catenin can induce a favorable tumor microenvironment. Thus, parallel activation of NF-κB and β-catenin signaling by gain-of-function mutations in CARMA1 augments WNT stimulation and is required for regulating the expression of distinct NF-κB target genes to trigger cell-intrinsic and extrinsic processes that promote DLBCL lymphomagenesis.

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Section: Methodsmentioning

confidence: 99%

Oncogenic CARMA1 couples NF-κB and β-catenin signaling in diffuse large B-cell lymphomas

et al. 2016

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“…Emerging studies indicate that AIP has roles outside of its well known regulation of AhR and the xenobiotic response. AIP can interact with the CARMA1 adaptor molecule in T lymphocytes and enhances CARMA1 binding to MALT1 and BCL-10 to promote T cell receptor-mediated NF-B activation and IL-2 production (40). In this study, we describe a novel function of AIP as a negative regulator of IRF7 and antiviral signaling.…”

mentioning

confidence: 87%

Aryl Hydrocarbon Receptor Interacting Protein Targets IRF7 to Suppress Antiviral Signaling and the Induction of Type I Interferon

Zhou

Lavorgna

Bowman

et al. 2015

Journal of Biological Chemistry

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Background: IRF7 is known as the master regulator of type I IFN production, yet little is known about its negative regulation. Results: AIP interacts with IRF7 and inhibits IRF7 nuclear localization. Conclusion: AIP suppresses virus-induced type I IFN production by targeting IRF7 for inactivation. Significance: Understanding IRF7 regulation is important to elucidate the host innate immune response to virus infection.

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“…CK1α is recruited through the Coiled-coil and ID ( 23 ). The preponderance of protein interactions occurs through the N-terminal half of CARD11 that includes the CARD, LATCH, and Coiled-coil, although the C-terminal PDZ-SH3-MAGUK region can bind the ADAP adapter ( 24 ) and AIP ( 25 ). In T cells, the site of CARD11 complex assembly appears to be the immunological synapse ( 26 , 27 ).…”

Section: Receptor-induced Recruitment Of Signaling Cofactorsmentioning

confidence: 99%

Mechanisms of Regulated and Dysregulated CARD11 Signaling in Adaptive Immunity and Disease

et al. 2018

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CARD11 functions as a key signaling scaffold that controls antigen-induced lymphocyte activation during the adaptive immune response. Somatic mutations in CARD11 are frequently found in Non-Hodgkin lymphoma, and at least three classes of germline CARD11 mutations have been described as the basis for primary immunodeficiency. In this review, we summarize our current understanding of how CARD11 signals, how its activity is regulated, and how mutations bypass normal regulation to cause disease.

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AIP augments CARMA1-BCL10-MALT1 complex formation to facilitate NF-κB signaling upon T cell activation

Cited by 21 publications

References 27 publications

Oncogenic CARMA1 couples NF-κB and β-catenin signaling in diffuse large B-cell lymphomas

Oncogenic CARMA1 couples NF-κB and β-catenin signaling in diffuse large B-cell lymphomas

Aryl Hydrocarbon Receptor Interacting Protein Targets IRF7 to Suppress Antiviral Signaling and the Induction of Type I Interferon

Mechanisms of Regulated and Dysregulated CARD11 Signaling in Adaptive Immunity and Disease

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