Met1-linked Ubiquitination in Immune Signalling

TY - JOUR

T1 - Met1-linked Ubiquitination in Immune Signalling

AU - Fiil, Berthe Katrine

AU - Gyrd-Hansen, Mads

N1 - This article is protected by copyright. All rights reserved.

PY - 2014/10/1

Y1 - 2014/10/1

N2 - 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.

AB - 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.

U2 - 10.1111/febs.12944

DO - 10.1111/febs.12944

M3 - Review

C2 - 25060092

SN - 1742-464X

VL - 81

SP - 4337

EP - 4350

JO - F E B S Journal

JF - F E B S Journal

IS - 19

ER -