Proteome-wide forced interactions reveal a functional map of cell-cycle phospho-regulation in S. cerevisiae
Dynamic protein phosphorylation and dephosphorylation play an essential role in cell cycle progression. Kinases and phosphatases are generally highly conserved across eukaryotes, underlining their importance for post-translational regulation of substrate proteins. In recent years, advances in phosph...
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Language: | English |
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Taylor & Francis Group
2024-12-01
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Online Access: | https://www.tandfonline.com/doi/10.1080/19491034.2024.2420129 |
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author | Cinzia Klemm Guðjón Ólafsson Henry Richard Wood Caitlin Mellor Nicolae Radu Zabet Peter Harold Thorpe |
author_facet | Cinzia Klemm Guðjón Ólafsson Henry Richard Wood Caitlin Mellor Nicolae Radu Zabet Peter Harold Thorpe |
author_sort | Cinzia Klemm |
collection | DOAJ |
description | Dynamic protein phosphorylation and dephosphorylation play an essential role in cell cycle progression. Kinases and phosphatases are generally highly conserved across eukaryotes, underlining their importance for post-translational regulation of substrate proteins. In recent years, advances in phospho-proteomics have shed light on protein phosphorylation dynamics throughout the cell cycle, and ongoing progress in bioinformatics has significantly improved annotation of specific phosphorylation events to a given kinase. However, the functional impact of individual phosphorylation events on cell cycle progression is often unclear. To address this question, we used the Synthetic Physical Interactions (SPI) method, which enables the systematic recruitment of phospho-regulators to most yeast proteins. Using this method, we identified several putative novel targets involved in chromosome segregation and cytokinesis. The SPI method monitors cell growth and, therefore, serves as a tool to determine the impact of protein phosphorylation on cell cycle progression. |
format | Article |
id | doaj-art-6d85e4dc72694e87b783eb2b145ec19d |
institution | Kabale University |
issn | 1949-1034 1949-1042 |
language | English |
publishDate | 2024-12-01 |
publisher | Taylor & Francis Group |
record_format | Article |
series | Nucleus |
spelling | doaj-art-6d85e4dc72694e87b783eb2b145ec19d2024-12-09T07:27:13ZengTaylor & Francis GroupNucleus1949-10341949-10422024-12-0115110.1080/19491034.2024.2420129Proteome-wide forced interactions reveal a functional map of cell-cycle phospho-regulation in S. cerevisiaeCinzia Klemm0Guðjón Ólafsson1Henry Richard Wood2Caitlin Mellor3Nicolae Radu Zabet4Peter Harold Thorpe5School of Biological and Behavioural Sciences, Queen Mary University of London, London, UKSchool of Biological and Behavioural Sciences, Queen Mary University of London, London, UKSchool of Biological and Behavioural Sciences, Queen Mary University of London, London, UKSchool of Biological and Behavioural Sciences, Queen Mary University of London, London, UKBlizard Institute, Barts and The London School of Medicine and Dentistry, Queen Mary University of London, London, UKSchool of Biological and Behavioural Sciences, Queen Mary University of London, London, UKDynamic protein phosphorylation and dephosphorylation play an essential role in cell cycle progression. Kinases and phosphatases are generally highly conserved across eukaryotes, underlining their importance for post-translational regulation of substrate proteins. In recent years, advances in phospho-proteomics have shed light on protein phosphorylation dynamics throughout the cell cycle, and ongoing progress in bioinformatics has significantly improved annotation of specific phosphorylation events to a given kinase. However, the functional impact of individual phosphorylation events on cell cycle progression is often unclear. To address this question, we used the Synthetic Physical Interactions (SPI) method, which enables the systematic recruitment of phospho-regulators to most yeast proteins. Using this method, we identified several putative novel targets involved in chromosome segregation and cytokinesis. The SPI method monitors cell growth and, therefore, serves as a tool to determine the impact of protein phosphorylation on cell cycle progression.https://www.tandfonline.com/doi/10.1080/19491034.2024.2420129Cdc5Cdc7CDKcell cyclephosphatasesphospho-regulation |
spellingShingle | Cinzia Klemm Guðjón Ólafsson Henry Richard Wood Caitlin Mellor Nicolae Radu Zabet Peter Harold Thorpe Proteome-wide forced interactions reveal a functional map of cell-cycle phospho-regulation in S. cerevisiae Nucleus Cdc5 Cdc7 CDK cell cycle phosphatases phospho-regulation |
title | Proteome-wide forced interactions reveal a functional map of cell-cycle phospho-regulation in S. cerevisiae |
title_full | Proteome-wide forced interactions reveal a functional map of cell-cycle phospho-regulation in S. cerevisiae |
title_fullStr | Proteome-wide forced interactions reveal a functional map of cell-cycle phospho-regulation in S. cerevisiae |
title_full_unstemmed | Proteome-wide forced interactions reveal a functional map of cell-cycle phospho-regulation in S. cerevisiae |
title_short | Proteome-wide forced interactions reveal a functional map of cell-cycle phospho-regulation in S. cerevisiae |
title_sort | proteome wide forced interactions reveal a functional map of cell cycle phospho regulation in s cerevisiae |
topic | Cdc5 Cdc7 CDK cell cycle phosphatases phospho-regulation |
url | https://www.tandfonline.com/doi/10.1080/19491034.2024.2420129 |
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