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Abd-Ellah, A.* ; Voogdt, C.* ; Krappmann, D. ; Möller, P.* ; Marienfeld, R.B.*

GSK3β modulates NF-κB activation and RelB degradation through site-specific phosphorylation of BCL10.

Sci. Rep. 8:1352 (2018)
Verlagsversion Forschungsdaten DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
Glycogen synthase kinase 3 beta (GSK3 beta) is a ubiquitously expressed serine/threonine kinase involved in the regulation of various cellular functions, such as energy homoeostasis, cell growth and developmental processes. More recently, GSK3 beta has been identified as a part of a protein complex involved in the regulation of the CARMA1-BCL10-MALT1 complex (CBM complex) formation, which is a key signalling event upon antigen receptor engagement of B and T cells, required for the activation of the NF-kappa B and JNK pathways. However, conflicting reports have been published regarding the role of GSK3 beta for the activation of the NF-kappa B signalling pathways. Therefore, we aimed to determine the impact of GSK3 beta on the NF-kappa B signalling induced upon T cell activation. Blocking GSK3 beta by either pharmacologic inhibitors (SB216763 and SB415286) or by RNAi caused a reduced proteolysis of the MALT1 targets CYLD1, BCL10 and RelB as well as diminished I kappa B alpha degradation, NF-kappa B DNA binding and NF-kappa B activity. This negative effect on NF-kappa B appears to be due to a diminished CBM complex formation caused by a reduced BCL10 phosphorylation. Taken together, we provide here evidence for a novel regulatory mechanism by which GSK3 beta affects NF-kappa B signalling in activated T cells.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Glycogen-synthase Kinase-3-beta; Cell-survival; Lymphoma; Malt1; Ikk; Inactivation; Lymphocytes; Complexes; Cleavage; Carma1
ISSN (print) / ISBN 2045-2322
e-ISSN 2045-2322
Zeitschrift Scientific Reports
Quellenangaben Band: 8, Heft: 1, Seiten: , Artikelnummer: 1352 Supplement: ,
Verlag Nature Publishing Group
Verlagsort London
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Research Unit Signaling and Translation (SAT)