Anna C. Schmukle

TL;DR: It is concluded that by enabling linear ubiquitination in the TNF receptor signalling complex, SHARPIN interferes with TNF-induced cell death and, thereby, prevents inflammation.

TL;DR: It is demonstrated that sustained stability of the T NF-RSC requires LUBAC's enzymatic activity, thereby adding a third form of ubiquitin linkage to the triggering of TNF signaling by the TNF-R SC.

TL;DR: Results show that TRAF2 has anti-apoptotic signaling roles in addition to promoting NF-κB signaling and that efficient activation of NF-σB by TNFR1 requires the recruitment of cIAP1/2 by TRAf2.

TL;DR: The covalent attachment of ubiquitin molecules to target proteins is a posttranslational modification that is involved not only in signaling processes leading to protein degradation but also in those resulting in activation, proliferation, and cell death.

TL;DR: This Commentary summarises the information that is currently available and incorporates it into a new model of NF-κB activation, thereby highlighting the emerging new challenges in understanding the role of ubiquitylation in NF-σB activation.