[en] 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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Barbour, Haithem; Biomedical Sciences Programs, University of Montreal, Montreal, QC H3C 3T5, Canada ; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada
Nkwe, Nadine Sen; Molecular Biology Programs, University of Montreal, Montreal, QC H3A 0G4, Canada ; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada
Estavoyer, Benjamin; Molecular Biology Programs, University of Montreal, Montreal, QC H3A 0G4, Canada ; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada
Messmer, Clémence; Department of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC H3C 3J7, Canada ; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada
Gushul-Leclaire, Mila; Department of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC H3C 3J7, Canada ; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada
Villot, Romain; Department of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC H3C 3J7, Canada ; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada
Uriarte, Maxime ; Université de Liège - ULiège > Département des sciences biomédicales et précliniques ; Department of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC H3C 3J7, Canada ; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada
Boulay, Karine; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada
Hlayhel, Sari; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada
Farhat, Bassel; Department of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC H3C 3J7, Canada ; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada
Milot, Eric ; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada ; Department of Medicine, University of Montréal, Montreal, QC H3C 3J7, Canada
Mallette, Frédérick A; Department of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC H3C 3J7, Canada ; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada ; Department of Medicine, University of Montréal, Montreal, QC H3C 3J7, Canada
Daou, Salima; Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, ON M5G 1X5, Canada
Affar, El Bachir ; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada ; Department of Medicine, University of Montréal, Montreal, QC H3C 3J7, Canada
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