Met1-linked ubiquitination in immune signalling

Journal article

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-κB 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.

Authors: Fiil, B; Gyrd-Hansen, M

• Publisher: Blackwell Publishing Ltd
• Journal: FEBS Journal
• Volume: 281
• Issue: 19
• Pages: 4337-4350
• Publication date: 2014-10-01
• DOI: 10.1111/febs.12944
• EISSN: 1742-4658
• ISSN: 1742-464X
• Language: English
• Keywords: NEMO; Immune receptor signalling; OTULIN; Met1-linked ubiquitin; Innate immunity; LUBAC; Inflammation