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泛素化修饰:一种类泛素修饰。

UFMylation: a ubiquitin-like modification.

机构信息

Inserm U1242, University of Rennes, Rennes, France; Centre de Lutte Contre le Cancer Eugène Marquis, Rennes, France.

Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.

出版信息

Trends Biochem Sci. 2024 Jan;49(1):52-67. doi: 10.1016/j.tibs.2023.10.004. Epub 2023 Nov 7.

Abstract

Post-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.

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