| First Author | De A | Year | 2014 |
| Journal | EMBO Rep | Volume | 15 |
| Issue | 7 | Pages | 775-83 |
| PubMed ID | 24878851 | Mgi Jnum | J:217021 |
| Mgi Id | MGI:5612927 | Doi | 10.15252/embr.201338305 |
| Citation | De A, et al. (2014) The deubiquitinase activity of A20 is dispensable for NF-kappaB signaling. EMBO Rep 15(7):775-83 |
| abstractText | A20 has been suggested to limit NF-kappaB activation by removing regulatory ubiquitin chains from ubiquitinated substrates. A20 is a ubiquitin-editing enzyme that removes K63-linked ubiquitin chains from adaptor proteins, such as RIP1, and then conjugates them to K48-linked polyubiquitin chains to trigger proteasomal degradation. To determine the role of the deubiquitinase function of A20 in downregulating NF-kappaB signaling, we have generated a knock-in mouse that lacks the deubiquitinase function of A20 (A20-OTU mice). These mice are normal and have no signs of inflammation, have normal proportions of B, T, dendritic, and myeloid cells, respond normally to LPS and TNF, and undergo normal NF-kappaB activation. Our results thus indicate that the deubiquitinase activity of A20 is dispensable for normal NF-kappaB signaling. |
