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

ABSTRACT:

Background

The CARMA1-BCL10-MALT1 (CBM) complex bridges T cell receptor (TCR) signaling to the canonical I?B kinase (IKK)/NF-?B pathway. The CBM complex constitutes a signaling cluster of more than 1 Mio Dalton. Little is known about factors that facilitate the rapid assembly and maintenance of this dynamic higher order complex.

Findings

Here, we report the novel interaction of the aryl hydrocarbon receptor (AHR) interacting protein (AIP) and the molecular scaffold protein CARMA1. In T cells, transient binding of CARMA1 and AIP enhanced formation of the CBM complex. Thereby, AIP promoted optimal IKK/NF-?B signaling and IL-2 production in response to TCR/CD28 co-stimulation.

Conclusions

Our data demonstrate that AIP acts as a positive regulator of NF-?B signaling upon T cell activation.

SUBMITTER: Schimmack G

PROVIDER: S-EPMC4222456 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature

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

Schimmack Gisela G Eitelhuber Andrea C AC Vincendeau Michelle M Demski Katrin K Shinohara Hisaaki H Kurosaki Tomohiro T Krappmann Daniel D

Cell communication and signaling : CCS 20140722

<h4>Background</h4>The CARMA1-BCL10-MALT1 (CBM) complex bridges T cell receptor (TCR) signaling to the canonical IκB kinase (IKK)/NF-κB pathway. The CBM complex constitutes a signaling cluster of more than 1 Mio Dalton. Little is known about factors that facilitate the rapid assembly and maintenance of this dynamic higher order complex.<h4>Findings</h4>Here, we report the novel interaction of the aryl hydrocarbon receptor (AHR) interacting protein (AIP) and the molecular scaffold protein CARMA1. ...[more]

PMID: 25245034

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