cIAP1/2 Regulates Ubiquitination of RIP1-4
Author Information
Author(s): Bertrand Mathieu J. M., Lippens Saskia, Staes An, Gilbert Barbara, Roelandt Ria, De Medts Jelle, Gevaert Kris, Declercq Wim, Vandenabeele Peter
Primary Institution: Department for Molecular Biomedical Research, VIB, Ghent, Belgium
Hypothesis
The study investigates the role of cIAP1 and cIAP2 as E3 ubiquitin ligases for RIP1-4 and their impact on NF-κB activation.
Conclusion
cIAP1 and cIAP2 are essential for the ubiquitination of RIP1-4, which regulates NF-κB activation.
Supporting Evidence
- cIAP1 and cIAP2 directly bind to RIP1, RIP2, RIP3, and RIP4.
- cIAP1 is capable of conjugating RIPs with diverse types of ubiquitin chains, including linear chains.
- Repressing cIAP1/2 levels affects the activation of NF-κB dependent on RIP1-4.
Takeaway
This study shows that certain proteins help attach small tags to other proteins, which is important for how cells respond to stress.
Methodology
The study used in vitro ubiquitination assays and co-immunoprecipitation experiments to analyze the interactions and ubiquitination of RIP proteins.
Digital Object Identifier (DOI)
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