CARMA1 is a critical lipid raft–associated regulator of TCR-induced NF-κB activation

Autor:	Claude Bron, Salvatore Valitutti, Daniel F. Legler, Brian Brissoni, David Bonnet, Olivier Gaide, Jürg Tschopp, Benoit Favier, Margot Thome
Rok vydání:	2002
Předmět:	Scaffold protein CARD Signaling Adaptor Proteins Guanylate kinase T cell Immunology T-cell receptor CD28 hemic and immune systems chemical and pharmacologic phenomena Biology Cell biology medicine.anatomical_structure ddc:570 medicine Immunology and Allergy Signal transduction Lipid raft
Zdroj:	Nature Immunology. 3:836-843
ISSN:	1529-2916 1529-2908
DOI:	10.1038/ni830
Popis:	CARMA1 is a lymphocyte-specific member of the membrane-associated guanylate kinase (MAGUK) family of scaffolding proteins, which coordinate signaling pathways emanating from the plasma membrane. CARMA1 interacts with Bcl10 via its caspase-recruitment domain (CARD). Here we investigated the role of CARMA1 in T cell activation and found that T cell receptor (TCR) stimulation induced a physical association of CARMA1 with the TCR and Bcl10. We found that CARMA1 was constitutively associated with lipid rafts, whereas cytoplasmic Bcl10 translocated into lipid rafts upon TCR engagement. A CARMA1 mutant, defective for Bcl10 binding, had a dominant-negative (DN) effect on TCR-induced NF-kappa B activation and IL-2 production and on the c-Jun NH(2)-terminal kinase (Jnk) pathway when the TCR was coengaged with CD28. Together, our data show that CARMA1 is a critical lipid raft-associated regulator of TCR-induced NF-kappa B activation and CD28 costimulation-dependent Jnk activation. published
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::966bbe533f9ad633e13944078ebc2618 https://doi.org/10.1038/ni830 Zobrazit plný text záznamu Plný text ve formátu PDF