期刊
MOLECULAR AND CELLULAR BIOLOGY
卷 33, 期 24, 页码 4971-4984出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.00465-13
关键词
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资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Grants-in-Aid for Scientific Research [22125005, 23370079] Funding Source: KAKEN
Tumor necrosis factor alpha (TNF-alpha) plays a role in apoptosis and proliferation in multiple types of cells, and defects in TNF-alpha induced apoptosis are associated with various autoimmune diseases. Here, we show that TRIM27, a tripartite motif (TRIM) protein containing RING finger, B-box, and coiled-coil domains, positively regulates TNF-alpha-induced apoptosis. Trim27-deficient mice are resistant to TNF-alpha-D-galactosamine-induced hepatocyte apoptosis. Trim27-deficient mouse embryonic fibroblasts (MEFs) are also resistant to TNF-alpha-cycloheximide-induced apoptosis. TRIM27 forms a complex with and ubiquitinates the ubiquitin-specific protease USP7, which deubiquitinates receptor-interacting protein 1 (RIP1), resulting in the positive regulation of TNF-alpha-induced apoptosis. Our findings indicate that the ubiquitination-deubiquitination cascade mediated by the TRIM27-USP7 complex plays an important role in TNF-alpha-induced apoptosis.
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