Ubiquitination at the crossroad of cell death and inflammation in health and disease
Ubiquitination, a versatile post-translational modification, plays a central role in regulating immune responses and cell fate decisions. Acting as a molecular switch, distinct ubiquitin linkages orchestrate signaling cascades that balance inflammation and programmed cell death. Among these, linear (M1-linked) and K63-linked ubiquitin chains are pivotal in modulating NF-κB and MAPK pathways, ensuring appropriate immune activation while preventing unwarranted cytotoxicity. Dysregulation of ubiquitin-mediated signaling, particularly involving E3 ligases like LUBAC, underlies a spectrum of inflammatory and degenerative diseases, including autoimmune disorders, cancer, and metabolic syndrome. My lab focuses on understanding how specific ubiquitination events at the interface of inflammation and cell death maintain tissue homeostasis—and how their disruption contributes to pathogenesis. Understanding this crosstalk opens new avenues for therapeutic targeting in diseases driven by chronic inflammation and cell death.
Announcement of the SysBio Talk of Jun.-Prof. Dr. Nieves Peltzer