SPATA 2 promotes CYLD activity and regulates TNF ‐induced NF ‐κB signaling and cell death

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SPATA2 promotes CYLD activity and regulates TNF-induced NF-κB signaling and cell death.

K63- and Met1-linked ubiquitylation are crucial posttranslational modifications for TNF receptor signaling. These non-degradative ubiquitylations are counteracted by deubiquitinases (DUBs), such as the enzyme CYLD, resulting in an appropriate signal strength, but the regulation of this process remains incompletely understood. Here, we describe an interaction partner of CYLD, SPATA2, which we id...

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Ubiquitination of RIP1 Regulates an NF-κB-Independent Cell-Death Switch in TNF Signaling

TNF receptor 1 (TNFR1) can trigger opposing responses within the same cell: a prosurvival response or a cell-death pathway [1, 2]. Cell survival requires NF-kB-mediated transcription of prosurvival genes [3–9]; apoptosis occurs if NF-kB signaling is blocked [5, 7–9]. Hence, activation of NF-kB acts as a cell-death switch during TNF signaling. This study demonstrates that the pathway includes an...

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CYLD Deubiquitinase Negatively Regulates High Glucose-Induced NF-κB Inflammatory Signaling in Mesangial Cells

Nuclear factor-kappa B (NF-κB) is the key part of multiple signal transduction of inflammation in the pathogenesis of diabetic nephropathy (DN). The ubiquitin-proteasome system is extensively involved in the regulation of the NF-κB pathway. Cylindromatosis (CYLD) has deubiquitinase activity and acts as a negative regulator of the NF-κB signaling pathway. However, the association between CYLD an...

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TRAF2 phosphorylation promotes NF-κB–dependent gene expression and inhibits oxidative stress-induced cell death

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ژورنال

عنوان ژورنال: EMBO reports

سال: 2016

ISSN: 1469-221X,1469-3178

DOI: 10.15252/embr.201642592