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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Main Authors: Cinzia Klemm, Guðjón Ólafsson, Henry Richard Wood, Caitlin Mellor, Nicolae Radu Zabet, Peter Harold Thorpe
Format: Article
Language:English
Published: Taylor & Francis Group 2024-12-01
Series:Nucleus
Subjects:
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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AT henryrichardwood proteomewideforcedinteractionsrevealafunctionalmapofcellcyclephosphoregulationinscerevisiae
AT caitlinmellor proteomewideforcedinteractionsrevealafunctionalmapofcellcyclephosphoregulationinscerevisiae
AT nicolaeraduzabet proteomewideforcedinteractionsrevealafunctionalmapofcellcyclephosphoregulationinscerevisiae
AT peterharoldthorpe proteomewideforcedinteractionsrevealafunctionalmapofcellcyclephosphoregulationinscerevisiae