An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes
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 l...
| Main Authors: | , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2023-05-01
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| Series: | iScience |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S258900422300353X |
| _version_ | 1827958098211373056 |
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| author | Haithem Barbour Nadine Sen Nkwe Benjamin Estavoyer Clémence Messmer Mila Gushul-Leclaire Romain Villot Maxime Uriarte Karine Boulay Sari Hlayhel Bassel Farhat Eric Milot Frédérick A. Mallette Salima Daou El Bachir Affar |
| author_facet | Haithem Barbour Nadine Sen Nkwe Benjamin Estavoyer Clémence Messmer Mila Gushul-Leclaire Romain Villot Maxime Uriarte Karine Boulay Sari Hlayhel Bassel Farhat Eric Milot Frédérick A. Mallette Salima Daou El Bachir Affar |
| author_sort | Haithem Barbour |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-09T15:30:14Z |
| format | Article |
| id | doaj.art-8268603610614df7a8f26515e242e596 |
| institution | Directory Open Access Journal |
| issn | 2589-0042 |
| language | English |
| last_indexed | 2024-04-09T15:30:14Z |
| publishDate | 2023-05-01 |
| publisher | Elsevier |
| record_format | Article |
| series | iScience |
| spelling | doaj.art-8268603610614df7a8f26515e242e5962023-04-28T08:56:11ZengElsevieriScience2589-00422023-05-01265106276An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processesHaithem Barbour0Nadine Sen Nkwe1Benjamin Estavoyer2Clémence Messmer3Mila Gushul-Leclaire4Romain Villot5Maxime Uriarte6Karine Boulay7Sari Hlayhel8Bassel Farhat9Eric Milot10Frédérick A. Mallette11Salima Daou12El Bachir Affar13Biomedical Sciences Programs, University of Montreal, Montreal, QC H3C 3T5, Canada; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, CanadaMolecular Biology Programs, University of Montreal, Montreal, QC H3A 0G4, Canada; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, CanadaMolecular Biology Programs, University of Montreal, Montreal, QC H3A 0G4, Canada; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, CanadaDepartment of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC H3C 3J7, Canada; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, CanadaDepartment of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC H3C 3J7, Canada; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, CanadaDepartment of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC H3C 3J7, Canada; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, CanadaDepartment of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC H3C 3J7, Canada; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, CanadaMaisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, CanadaMaisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, CanadaDepartment of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC H3C 3J7, Canada; Maisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, CanadaMaisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada; Department of Medicine, University of Montréal, Montreal, QC H3C 3J7, Canada; Corresponding authorDepartment 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; Corresponding authorLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, ON M5G 1X5, Canada; Corresponding authorMaisonneuve-Rosemont Hospital Research Center, Montréal, QC H1T 2M4, Canada; Department of Medicine, University of Montréal, Montreal, QC H3C 3J7, Canada; Corresponding authorSummary: 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.http://www.sciencedirect.com/science/article/pii/S258900422300353XBiological sciencesBiochemistryMolecular biologyCell biology |
| spellingShingle | Haithem Barbour Nadine Sen Nkwe Benjamin Estavoyer Clémence Messmer Mila Gushul-Leclaire Romain Villot Maxime Uriarte Karine Boulay Sari Hlayhel Bassel Farhat Eric Milot Frédérick A. Mallette Salima Daou El Bachir Affar An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes iScience Biological sciences Biochemistry Molecular biology Cell biology |
| title | An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes |
| title_full | An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes |
| title_fullStr | An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes |
| title_full_unstemmed | An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes |
| title_short | An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes |
| title_sort | inventory of crosstalk between ubiquitination and other post translational modifications in orchestrating cellular processes |
| topic | Biological sciences Biochemistry Molecular biology Cell biology |
| url | http://www.sciencedirect.com/science/article/pii/S258900422300353X |
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