title: Met1-linked ubiquitination in immune signalling.
abstract: 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: Department of Disease Biology, Novo Nordisk Foundation Centre for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Denmark.
authors: Berthe K
authors: BK
authors: Fiil
authors: Mads
authors: M
authors: Gyrd-Hansen
mesh_terms: D000818:Animals; D006801:Humans; D007113:Immunity, Innate; D008715:Methionine / Q000378:metabolism*; D015398:Signal Transduction / Q000276:immunology*; D025801:Ubiquitin / Q000378:metabolism; D057149:Ubiquitinated Proteins / Q000378:metabolism; D054875:Ubiquitination
chemical_list: C479419:UBB protein, human; D025801:Ubiquitin; D057149:Ubiquitinated Proteins; D008715:Methionine
keywords: LUBAC; Met1-linked ubiquitin; NEMO; OTULIN; immune receptor signalling; inflammation; innate immunity