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

Research output: Contribution to journal › Journal article › Research › peer-review

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SPATA2 links CYLD to the TNF-α receptor signaling complex and modulates the receptor signaling outcomes. / Wagner, Sebastian A; Satpathy, Shankha; Beli, Petra; Choudhary, Chuna Ram.

In: E M B O Journal, Vol. 35, No. 17, 01.09.2016, p. 1868-1884.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Wagner, SA, Satpathy, S, Beli, P & Choudhary, CR 2016, 'SPATA2 links CYLD to the TNF-α receptor signaling complex and modulates the receptor signaling outcomes', E M B O Journal, vol. 35, no. 17, pp. 1868-1884. https://doi.org/10.15252/embj.201694300

APA

Wagner, S. A., Satpathy, S., Beli, P., & Choudhary, C. R. (2016). SPATA2 links CYLD to the TNF-α receptor signaling complex and modulates the receptor signaling outcomes. E M B O Journal, 35(17), 1868-1884. https://doi.org/10.15252/embj.201694300

Vancouver

Wagner SA, Satpathy S, Beli P, Choudhary CR. SPATA2 links CYLD to the TNF-α receptor signaling complex and modulates the receptor signaling outcomes. E M B O Journal. 2016 Sep 1;35(17):1868-1884. https://doi.org/10.15252/embj.201694300

Author

Wagner, Sebastian A ; Satpathy, Shankha ; Beli, Petra ; Choudhary, Chuna Ram. / SPATA2 links CYLD to the TNF-α receptor signaling complex and modulates the receptor signaling outcomes. In: E M B O Journal. 2016 ; Vol. 35, No. 17. pp. 1868-1884.

Bibtex

@article{8e83f51af10a48fb9ebeb22968799887,
title = "SPATA2 links CYLD to the TNF-α receptor signaling complex and modulates the receptor signaling outcomes",
abstract = "TNF-α is a key regulator of innate immune and proinflammatory responses. However, the composition of the TNF-α 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-α stimulation induces widespread protein phosphorylation and that the scope of phosphorylation expands in a temporal manner. TNF-α 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 TNF-RSC 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-κB and inhibits TNF-α-induced necroptosis, pointing to an important function of SPATA2 in modulating the outcomes of TNF-α signaling. Taken together, our study draws a detailed map of TNF-α signaling, identifies SPATA2 as a novel component of TNF-α signaling, and provides a rich resource for further functional investigations.",
author = "Wagner, {Sebastian A} and Shankha Satpathy and Petra Beli and Choudhary, {Chuna Ram}",
note = "{\textcopyright} 2016 The Authors.",
year = "2016",
month = sep,
day = "1",
doi = "10.15252/embj.201694300",
language = "English",
volume = "35",
pages = "1868--1884",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
number = "17",

}

RIS

TY - JOUR

T1 - SPATA2 links CYLD to the TNF-α receptor signaling complex and modulates the receptor signaling outcomes

AU - Wagner, Sebastian A

AU - Satpathy, Shankha

AU - Beli, Petra

AU - Choudhary, Chuna Ram

N1 - © 2016 The Authors.

PY - 2016/9/1

Y1 - 2016/9/1

N2 - TNF-α is a key regulator of innate immune and proinflammatory responses. However, the composition of the TNF-α 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-α stimulation induces widespread protein phosphorylation and that the scope of phosphorylation expands in a temporal manner. TNF-α 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 TNF-RSC 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-κB and inhibits TNF-α-induced necroptosis, pointing to an important function of SPATA2 in modulating the outcomes of TNF-α signaling. Taken together, our study draws a detailed map of TNF-α signaling, identifies SPATA2 as a novel component of TNF-α signaling, and provides a rich resource for further functional investigations.

AB - TNF-α is a key regulator of innate immune and proinflammatory responses. However, the composition of the TNF-α 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-α stimulation induces widespread protein phosphorylation and that the scope of phosphorylation expands in a temporal manner. TNF-α 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 TNF-RSC 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-κB and inhibits TNF-α-induced necroptosis, pointing to an important function of SPATA2 in modulating the outcomes of TNF-α signaling. Taken together, our study draws a detailed map of TNF-α signaling, identifies SPATA2 as a novel component of TNF-α signaling, and provides a rich resource for further functional investigations.

U2 - 10.15252/embj.201694300

DO - 10.15252/embj.201694300

M3 - Journal article

C2 - 27307491

VL - 35

SP - 1868

EP - 1884

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 17

ER -

ID: 162643966