The proteolytic activity of the paracaspase MALT1 is key in T cell activation.
Rebeaud, Fabien; Hailfinger, Stephan; Posevitz-Fejfar, Anita; Tapernoux, Myriam; Moser, Roger; Rueda, Daniel; Gaide, Olivier; Guzzardi, Montserrat; Iancu, Emanuela M; Rufer, Nathalie; Fasel, Nicolas; Thome, Margot.
; 9(3): 272-81, 2008 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-18264101
T cell antigen receptor stimulation induces MALT1 paracaspase-mediated cleavage of the NF-kappaB inhibitor A20.
The protease activity of the paracaspase MALT1 is controlled by monoubiquitination.
An allosteric MALT1 inhibitor is a molecular corrector rescuing function in an immunodeficient patient.
MicroRNA-649 promotes HSV-1 replication by directly targeting MALT1.
Selective autophagy of the adaptor protein Bcl10 modulates T cell receptor activation of NF-κB.
B-cell receptor-driven MALT1 activity regulates MYC signaling in mantle cell lymphoma.
Malt1-induced cleavage of regnase-1 in CD4(+) helper T cells regulates immune activation.
T-cell receptor-induced JNK activation requires proteolytic inactivation of CYLD by MALT1.
Ca2+/calmodulin-dependent kinase II contributes to inhibitor of nuclear factor-kappa B kinase complex activation in Helicobacter pylori infection.
COP9 signalosome controls the Carma1-Bcl10-Malt1 complex upon T-cell stimulation.