An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes

Ubiquitination is an important post-translational modification (PTM) that regulates a large spectrum of cellular processes in eukaryotes. Abnormalities in ubiquitin signaling underlie numerous human pathologies including cancer and neurodegeneration. Much progress has been made during the last three...

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Bibliographic Details
Published in:	iScience Vol. 26; no. 5; p. 106276
Main Authors:	Barbour, Haithem, Nkwe, Nadine Sen, Estavoyer, Benjamin, Messmer, Clémence, Gushul-Leclaire, Mila, Villot, Romain, Uriarte, Maxime, Boulay, Karine, Hlayhel, Sari, Farhat, Bassel, Milot, Eric, Mallette, Frédérick A., Daou, Salima, Affar, El Bachir
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 19-05-2023 Elsevier
Subjects:	Biochemistry Biological sciences Cell biology Molecular biology Review Cell biology Biological sciences Biochemistry Molecular biology
Online Access:	Get full text
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Summary:	Ubiquitination is an important post-translational modification (PTM) that regulates a large spectrum of cellular processes in eukaryotes. Abnormalities in ubiquitin signaling underlie numerous human pathologies including cancer and neurodegeneration. Much progress has been made during the last three decades in understanding how ubiquitin ligases recognize their substrates and how ubiquitination is orchestrated. Several mechanisms of regulation have evolved to prevent promiscuity including the assembly of ubiquitin ligases in multi-protein complexes with dedicated subunits and specific post-translational modifications of these enzymes and their co-factors. Here, we outline another layer of complexity involving the coordinated access of E3 ligases to substrates. We provide an extensive inventory of ubiquitination crosstalk with multiple PTMs including SUMOylation, phosphorylation, methylation, acetylation, hydroxylation, prolyl isomerization, PARylation, and O-GlcNAcylation. We discuss molecular mechanisms by which PTMs orchestrate ubiquitination, thus increasing its specificity as well as its crosstalk with other signaling pathways to ensure cell homeostasis. [Display omitted] Biological sciences; Biochemistry; Molecular biology; Cell biology
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 These authors contributed equally
ISSN:	2589-0042 2589-0042
DOI:	10.1016/j.isci.2023.106276