protein-protein interaction dataset TNFR1-mediated NFkB signaling

Most MS-based approaches to study protein-protein interactions require homogenization of the cells, which leads to loss of the cellular structures, dilution of proteins and formation of incorrect protein complexes. Furthermore, several purification and washing steps are needed, which can lead to the loss of (weaker) interactions. We recently developed a new method for studying protein complexes without interfering with the cellular integrity; Virotrap. By trapping and purifying protein complexes in virus-like particles, we avoid cell lysis and preserve intact complexes during the purification process. Here, we present a protein-protein interaction network of the TNFR1-induced NF-κB and apoptosis pathway, using TRADD, FADD, TRAF2, cIAP1, NEMO, TANK, HOIL1, HOIP, SHARPIN, A20, ABIN1 and ABIN2 as baits in Virotrap. Virotrap was applied both under resting conditions as well as upon TNF stimulation, which reveals dynamic interactions in TNFR1-induced NF-κB signaling. The found interactions compromise both known interactors as well as novel ones that might serve as valuable resource for further unraveling the molecular mechanisms controlling inflammation, cellular proliferation and cell death.