IAP-Mediated Protein Ubiquitination in Regulating Cell Signaling.
Fiche publication
Date publication
avril 2020
Journal
Cells
Auteurs
Membres identifiés du Cancéropôle Est :
Dr DUBREZ Laurence
Tous les auteurs :
Dumétier B, Zadoroznyj A, Dubrez L
Lien Pubmed
Résumé
Over the last decade, the E3-ubiquitine ligases from IAP (Inhibitor of Apoptosis) family have emerged as potent regulators of immune response. In immune cells, they control signaling pathways driving differentiation and inflammation in response to stimulation of tumor necrosis factor receptor (TNFR) family, pattern-recognition receptors (PRRs), and some cytokine receptors. They are able to control the activity, the cellular fate, or the stability of actors of signaling pathways, acting at different levels from components of receptor-associated multiprotein complexes to signaling effectors and transcription factors, as well as cytoskeleton regulators. Much less is known about ubiquitination substrates involved in non-immune signaling pathways. This review aimed to present IAP ubiquitination substrates and the role of IAP-mediated ubiquitination in regulating signaling pathways.
Mots clés
IAP, cell signaling, inflammation, ubiquitination
Référence
Cells. 2020 Apr 30;9(5):