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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.

Original publication

DOI

10.1111/febs.12944

Type

Journal article

Journal

FEBS J

Publication Date

10/2014

Volume

281

Pages

4337 - 4350

Keywords

LUBAC, Met1-linked ubiquitin, NEMO, OTULIN, immune receptor signalling, inflammation, innate immunity, Animals, Humans, Immunity, Innate, Methionine, Signal Transduction, Ubiquitin, Ubiquitinated Proteins, Ubiquitination