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Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
Published on: May 10, 2022
UXT-V1 protects cells against TNF-induced apoptosis through modulating complex II formation
Yuefeng Huang1, Liang Chen, Yi Zhou
1Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Molecular Biology of the Cell
|February 11, 2011
Summary
UXT-V1, a novel protein, regulates tumor necrosis factor (TNF)-induced apoptosis by interacting with TNF receptor signaling components. Its degradation promotes cell death, revealing a new mechanism in apoptosis regulation.
Area of Science:
- Cell Biology
- Molecular Biology
- Immunology
Background:
- Tumor necrosis factor (TNF) signaling is crucial for cell death and survival.
- Ubiquitously expressed transcript (UXT) isoforms play roles in cellular regulation.
- UXT-V2 regulates nuclear factor-κB in the nucleus.
Purpose of the Study:
- To investigate the role of UXT-V1, a cytoplasmic isoform of UXT, in TNF-induced apoptosis.
- To elucidate the molecular mechanism by which UXT-V1 regulates TNF signaling.
Main Methods:
- Cellular localization studies of UXT-V1.
- Knockdown experiments to assess sensitivity to TNF.
- Co-immunoprecipitation assays to identify binding partners.
- Analysis of protein degradation and complex formation.
Main Results:
- UXT-V1 localizes in the cytoplasm and regulates TNF-induced apoptosis.
- UXT-V1 knockdown increases sensitivity to TNF-induced cell death.
- UXT-V1 binds to TNF receptor-associated factor 2 (TRAF2).
- UXT-V1 prevents the recruitment of TNF receptor-associated death domain (TRADD) to the TNF receptor.
- Degradation of UXT-V1 facilitates the formation of apoptotic receptor complex II.
Conclusions:
- UXT-V1 is a novel cytoplasmic regulator of TNF-induced apoptosis.
- UXT-V1 acts as a negative regulator by preventing early signaling complex assembly.
- The degradation of UXT-V1 is a key step in initiating TNF-induced apoptosis.
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