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AIP augments CARMA1-BCL10-MALT1 complex formation to facilitate NF-kappa B signaling upon T cell activation.
Cell Commun. Signal. 12:49 (2014)
Background: The CARMA1-BCL10-MALT1 (CBM) complex bridges T cell receptor (TCR) signaling to the canonical I kappa B kinase (IKK)/NF-kappa 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-kappa 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-kappa B signaling upon T cell activation.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Immunology ; T Cell Signaling ; Canonical Nf-kappa B ; Maguk Family; Aryl-hydrocarbon Receptor; Guanylate Kinase Domains; Ah Receptor; Protein; Carma1; Phosphorylation; Xap2
ISSN (print) / ISBN
1478-811X
e-ISSN
1478-811X
Journal
Cell Communication and Signaling
Quellenangaben
Volume: 12,
Issue: 1,
Article Number: 49
Publisher
BioMed Central
Publishing Place
London
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Research Unit Signaling and Translation (SAT)