In JoVE (1)
Other Publications (1)
Articles by Mathieu Dondelinger in JoVE
The Use of a β-lactamase-based Conductimetric Biosensor Assay to Detect Biomolecular Interactions Marylène Vandevenne*1, Mathieu Dondelinger*1, Sami Yunus2, Astrid Freischels1, Régine Freischels1, Oscar Crasson1, Noureddine Rhazi1, Pierre Bogaerts3, Moreno Galleni1, Patrice Filée4 1Life Science Department, University of Liège, 2Institute of Condensed Matter and Nanoscience, Catholic University of Louvain, 3Laboratory of Clinical Microbiology, Catholic University of Louvain, 4Biotechnology Department, CER Group In this work, we report a new method to study protein-protein interactions using a conductimetric biosensor based on the hybrid β-lactamase technology. This method relies on release of protons upon hydrolysis of β-lactams.
Other articles by Mathieu Dondelinger on PubMed
NF-κB-Independent Role of IKKα/IKKβ in Preventing RIPK1 Kinase-Dependent Apoptotic and Necroptotic Cell Death During TNF Signaling Molecular Cell. | Pubmed ID: 26344099 TNF is a master pro-inflammatory cytokine. Activation of TNFR1 by TNF can result in both RIPK1-independent apoptosis and RIPK1 kinase-dependent apoptosis or necroptosis. These cell death outcomes are regulated by two distinct checkpoints during TNFR1 signaling. TNF-mediated NF-κB-dependent induction of pro-survival or anti-apoptotic molecules is a well-known late checkpoint in the pathway, protecting cells from RIPK1-independent death. On the other hand, the molecular mechanism regulating the contribution of RIPK1 to cell death is far less understood. We demonstrate here that the IKK complex phosphorylates RIPK1 at TNFR1 complex I and protects cells from RIPK1 kinase-dependent death, independent of its function in NF-κB activation. We provide in vitro and in vivo evidence that inhibition of IKKα/IKKβ or its upstream activators sensitizes cells to death by inducing RIPK1 kinase-dependent apoptosis or necroptosis. We therefore report on an unexpected, NF-κB-independent role for the IKK complex in protecting cells from RIPK1-dependent death downstream of TNFR1.