Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1)

Abstract Rif1 is a conserved protein that plays essential roles in orchestrating DNA replication timing, controlling nuclear architecture, telomere length and DNA repair. However, the relationship between these different roles, as well as the molecular basis of Rif1 function is still unclear. The as...

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Autores principales:	Rasa Sukackaite, Daniela Cornacchia, Malene Ringkjøbing Jensen, Philippe J. Mas, Martin Blackledge, Elin Enervald, Guangyou Duan, Tania Auchynnikava, Maja Köhn, Darren J. Hart, Sara B. C. Buonomo
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9f35b459fd38478fae9ae9719311f2f5
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spelling	oai:doaj.org-article:9f35b459fd38478fae9ae9719311f2f52021-12-02T12:31:59ZMouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1)10.1038/s41598-017-01910-12045-2322https://doaj.org/article/9f35b459fd38478fae9ae9719311f2f52017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01910-1https://doaj.org/toc/2045-2322Abstract Rif1 is a conserved protein that plays essential roles in orchestrating DNA replication timing, controlling nuclear architecture, telomere length and DNA repair. However, the relationship between these different roles, as well as the molecular basis of Rif1 function is still unclear. The association of Rif1 with insoluble nuclear lamina has thus far hampered exhaustive characterization of the associated protein complexes. We devised a protocol that overcomes this problem, and were thus able to discover a number of novel Rif1 interactors, involved in chromatin metabolism and phosphorylation. Among them, we focus here on PP1. Data from different systems have suggested that Rif1-PP1 interaction is conserved and has important biological roles. Using mutagenesis, NMR, isothermal calorimetry and surface plasmon resonance we demonstrate that Rif1 is a high-affinity PP1 adaptor, able to out-compete the well-established PP1-inhibitor I2 in vitro. Our conclusions have important implications for understanding Rif1 diverse roles and the relationship between the biological processes controlled by Rif1.Rasa SukackaiteDaniela CornacchiaMalene Ringkjøbing JensenPhilippe J. MasMartin BlackledgeElin EnervaldGuangyou DuanTania AuchynnikavaMaja KöhnDarren J. HartSara B. C. BuonomoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Rasa Sukackaite Daniela Cornacchia Malene Ringkjøbing Jensen Philippe J. Mas Martin Blackledge Elin Enervald Guangyou Duan Tania Auchynnikava Maja Köhn Darren J. Hart Sara B. C. Buonomo Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1)
description	Abstract Rif1 is a conserved protein that plays essential roles in orchestrating DNA replication timing, controlling nuclear architecture, telomere length and DNA repair. However, the relationship between these different roles, as well as the molecular basis of Rif1 function is still unclear. The association of Rif1 with insoluble nuclear lamina has thus far hampered exhaustive characterization of the associated protein complexes. We devised a protocol that overcomes this problem, and were thus able to discover a number of novel Rif1 interactors, involved in chromatin metabolism and phosphorylation. Among them, we focus here on PP1. Data from different systems have suggested that Rif1-PP1 interaction is conserved and has important biological roles. Using mutagenesis, NMR, isothermal calorimetry and surface plasmon resonance we demonstrate that Rif1 is a high-affinity PP1 adaptor, able to out-compete the well-established PP1-inhibitor I2 in vitro. Our conclusions have important implications for understanding Rif1 diverse roles and the relationship between the biological processes controlled by Rif1.
format	article
author	Rasa Sukackaite Daniela Cornacchia Malene Ringkjøbing Jensen Philippe J. Mas Martin Blackledge Elin Enervald Guangyou Duan Tania Auchynnikava Maja Köhn Darren J. Hart Sara B. C. Buonomo
author_facet	Rasa Sukackaite Daniela Cornacchia Malene Ringkjøbing Jensen Philippe J. Mas Martin Blackledge Elin Enervald Guangyou Duan Tania Auchynnikava Maja Köhn Darren J. Hart Sara B. C. Buonomo
author_sort	Rasa Sukackaite
title	Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1)
title_short	Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1)
title_full	Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1)
title_fullStr	Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1)
title_full_unstemmed	Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1)
title_sort	mouse rif1 is a regulatory subunit of protein phosphatase 1 (pp1)
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/9f35b459fd38478fae9ae9719311f2f5
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Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1)

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