Met1-linked Ubiquitination in Immune Signalling
Research output: Contribution to journal › Review › Research › peer-review
Standard
Met1-linked Ubiquitination in Immune Signalling. / Fiil, Berthe Katrine; Gyrd-Hansen, Mads.
In: F E B S Journal, Vol. 81, No. 19, 10.2014, p. 4337-50.Research output: Contribution to journal › Review › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
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
Y1 - 2014/10
N2 - Methionine 1-linked ubiquitin chains (Met1-Ub), or linear ubiquitin, has emerged as a central post-translational modification in innate immune signalling. Molecular machinery that assembles, senses and, more recently, disassembles Met1-Ub has been identified, and technical advances have enabled identification of physiological substrates for Met1-Ub in response to activation of innate immune receptors. These discoveries have significantly advanced our understanding of how non-degradative ubiquitin modifications control pro-inflammatory responses mediated by nuclear factor κB and mitogen-activated protein kinases. In this review, we will discuss the current data on Met1-Ub function and regulation, and will point to some of the questions that still remain unanswered. This article is protected by copyright. All rights reserved.
AB - Methionine 1-linked ubiquitin chains (Met1-Ub), or linear ubiquitin, has emerged as a central post-translational modification in innate immune signalling. Molecular machinery that assembles, senses and, more recently, disassembles Met1-Ub has been identified, and technical advances have enabled identification of physiological substrates for Met1-Ub in response to activation of innate immune receptors. These discoveries have significantly advanced our understanding of how non-degradative ubiquitin modifications control pro-inflammatory responses mediated by nuclear factor κB and mitogen-activated protein kinases. In this review, we will discuss the current data on Met1-Ub function and regulation, and will point to some of the questions that still remain unanswered. This article is protected by copyright. All rights reserved.
U2 - 10.1111/febs.12944
DO - 10.1111/febs.12944
M3 - Review
C2 - 25060092
VL - 81
SP - 4337
EP - 4350
JO - F E B S Journal
JF - F E B S Journal
SN - 1742-464X
IS - 19
ER -
ID: 119770895