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

Rasa Sukackaite, Daniela Cornacchia, Malene Ringkjobing Jensen, Philippe J Mas, Martin Blackledge, Elin Enervald, Guangyou Duan, Tania Auchynnikava, Maja Kohn, Darren J Hart, Sara B.C. Buonomo

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Rif1 is a conserved protein, playing an essential role 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.
Original languageEnglish
Article number2119
Number of pages10
JournalScientific Reports
Issue number1
Publication statusPublished - 18 May 2017

Keywords / Materials (for Non-textual outputs)

  • Rif1
  • protein phosphatase 1 (PP1)
  • adaptor protein


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