| First Author | Zaman MM | Year | 2013 |
| Journal | Mol Cell Biol | Volume | 33 |
| Issue | 24 | Pages | 4971-84 |
| PubMed ID | 24144979 | Mgi Jnum | J:206755 |
| Mgi Id | MGI:5551943 | Doi | 10.1128/MCB.00465-13 |
| Citation | Zaman MM, et al. (2013) Ubiquitination-deubiquitination by the TRIM27-USP7 complex regulates tumor necrosis factor alpha-induced apoptosis. Mol Cell Biol 33(24):4971-84 |
| abstractText | 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. |
