Related Experiment Video
Updated: Mar 6, 2026

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
Published on: August 10, 2021
SPATA2: more than a missing link
Lisa Schlicher1,2,3, Prisca Brauns-Schubert1,2,3, Florian Schubert1,2,3
1Institute of Molecular Medicine and Cell Research, Albert-Ludwigs-University Freiburg, Stefan Meier Strasse 17, Freiburg 79104, Germany.
Abstract:
The assembly of the TNFR1 signalling complex (TNF-RSC) depends on K63- and M1-linked ubiquitylation, promoting the recruitment of complex constituents and the stability of the complex. Ubiquitylation is a dynamic process, controlled by E3 ubiquitin ligases as well as deubiquitinases, such as CYLD and OTULIN. A novel molecule, SPATA2, which is crucial for recruiting and activating the deubiquitinase CYLD within the TNF-RSC, has now been identified by four different studies. Loss of SPATA2 was shown to result in increased TNF-, but also NOD2-mediated proinflammatory signalling. Importantly, SPATA2 is instrumental for TNF-induced cell death, and a closer look at these findings suggests that SPATA2 possibly has functions beyond promoting the activity of CYLD.
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