UFMylation: a ubiquitin-like modification

Trends Biochem Sci. 2023 Nov 7:S0968-0004(23)00259-1. doi: 10.1016/j.tibs.2023.10.004. Online ahead of print.ABSTRACTPost-translational modifications (PTMs) add a major degree of complexity to the proteome and are essential controllers of protein homeostasis. Amongst the hundreds of PTMs identified, ubiquitin and ubiquitin-like (UBL) modifications are recognized as key regulators of cellular processes through their ability to affect protein-protein interactions, protein stability, and thus the functions of their protein targets. Here, we focus on the most recently identified UBL, ubiquitin-fold modifier 1 (UFM1), and the machinery responsible for its transfer to substrates (UFMylation) or its removal (deUFMylation). We first highlight the biochemical peculiarities of these processes, then we develop on how UFMylation and its machinery control various intertwined cellular processes and we highlight some of the outstanding research questions in this emerging field.PMID:37945409 | DOI:10.1016/j.tibs.2023.10.004

Source: Trends in Biochemical Sciences - November 9, 2023 Category: Biochemistry Authors: Xingchen Zhou Sayyed J Mahdizadeh Matthieu Le Gallo Leif A Eriksson Eric Chevet Elodie Lafont Source Type: research