Premium
Met1‐linked ubiquitination in immune signalling
Author(s) -
Fiil Berthe K.,
GyrdHansen Mads
Publication year - 2014
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12944
Subject(s) - ubiquitin , biology , immune system , innate immune system , signalling , microbiology and biotechnology , signal transduction , computational biology , genetics , gene
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.