MassIVE MSV000080842

Imported Reanalysis Dataset Public PXD003627

SPATA2 links CYLD to the TNF-a receptor signaling complex and modulates the receptor signaling outcomes

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Description

TNF-a is a key regulator of innate immune and proinflammatory responses. However, the composition of the TNF-a receptor associated signaling complexes (TNF-RSC) and the architecture of the downstream signaling networks are incompletely understood. We employed quantitative mass spectrometry to demonstrate that TNF-a stimulation induces widespread protein phosphorylation and that the scope of phosphorylation expands in a temporal manner. TNF-a stimulation also induces rapid ubiquitylation of components of the TNF-RSC. Temporal analysis of the TNF-RSC composition identified SPATA2 as a novel component of the TNFRSC. The predicted PUB domain in the N-terminus of SPATA2 interacts with the USP domain of CYLD, whereas the C-terminus of SPATA2 interacts with HOIP. SPATA2 is required for recruitment of CYLD to the TNF-RSC. Downregulation of SPATA2 augments transcriptional activation of NF-jB and inhibits TNF-a-induced necroptosis, pointing to an important function of SPATA2 in modulating the outcomes of TNF-a signaling. Taken together, our study draws a detailed map of TNF-a signaling, identifies SPATA2 as a novel component of TNF-a signaling, and provides a rich resource for further functional investigations. [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: TNF-alpha ; NF-kappaB ; necroptosis ; ubiquitin ; phosphorylation

Contact

Principal Investigators:
(in alphabetical order) 		Petra Beli, Institute of Molecular Biology (IMB), Mainz, Germany, N/A
Submitting User: ccms
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