| First Author | Fiil BK | Year | 2014 |
| Journal | FEBS J | Volume | 281 |
| Issue | 19 | Pages | 4337-50 |
| PubMed ID | 25060092 | Mgi Jnum | J:229223 |
| Mgi Id | MGI:5751057 | Doi | 10.1111/febs.12944 |
| Citation | Fiil BK, et al. (2014) Met1-linked ubiquitination in immune signalling. FEBS J 281(19):4337-50 |
| abstractText | N-terminal methionine-linked ubiquitin (Met1-Ub), or linear ubiquitin, has emerged as a central post-translational modification in innate immune signalling. The molecular machinery that assembles, senses and, more recently, disassembles Met1-Ub has been identified, and technical advances have enabled the identification of physiological substrates for Met1-Ub in response to activation of innate immune receptors. These discoveries have significantly advanced our understanding of how nondegradative ubiquitin modifications control proinflammatory responses mediated by nuclear factor-kappaB and mitogen-activated protein kinases. In this review, we discuss the current data on Met1-Ub function and regulation, and point to some of the questions that still remain unanswered. |
