SPOP promotes FADD degradation and inhibits NF-κB activity in non-small cell lung cancer
- Department of Oncology, The Third Affiliated Hospital of Soochow University, Changzhou, 213003 (China)
- Department of Oncology, Shanghai Pulmonary Hospital, Tongji University School of Medicine, Shanghai, 200433 (China)
- Department of Pathology, Shanghai Pulmonary Hospital, Tongji University School of Medicine, Shanghai, 200433 (China)
Highlights: • FADD protein level predicts poor prognosis of NSCLC patients. • SPOP binds to FADD and mediates its degradation. • SPOP inhibits NF-κB activity and its target genes expression. FAS-associated protein with death domain (FADD) is the pivotal adaptor protein, which transmits apoptotic signals mediated by the death receptors. Here we report that high FADD protein level predicts poor prognosis of non-small cell lung cancer (NSCLC) patients and its protein level is mainly regulated by the 26S proteasome. We also found that ubiquitin ligase SPOP (speckle-type POZ protein) binds to FADD and mediates its degradation, which can be blocked by MG132 treatment. Notably, SPOP inhibits NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) activity and its target genes expression via FADD. These results reveal the function of SPOP-FADDNFκB axis in NSCLC cells, which is associated with prognosis of NSCLC patients.
- OSTI ID:
- 23103550
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 504, Issue 1; Other Information: Copyright (c) 2018 Elsevier Inc. All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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