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Bora phosphorylation substitutes in trans for T-loop phosphorylation in Aurora A to promote mitotic entry

Authors
  • Tavernier, N.1, 2
  • Thomas, Y.2
  • Vigneron, S.3
  • Maisonneuve, P.1
  • Orlicky, S.1
  • Mader, P.1
  • Regmi, S. G.4
  • Van Hove, L.2
  • Levinson, N. M.5
  • Gasmi-Seabrook, G.6
  • Joly, N.2
  • Poteau, M.7
  • Velez-Aguilera, G.2
  • Gavet, O.7
  • Castro, A.3
  • Dasso, M.4
  • Lorca, T.3
  • Sicheri, F.1, 8, 8
  • Pintard, L.2
  • 1 Centre for Systems Biology, Lunenfeld Tanenbaum Research Institute, Sinai Health System, Toronto, ON, Canada , Toronto (Canada)
  • 2 Programme équipe Labellisée Ligue Contre le Cancer, Institut Jacques Monod, UMR7592, Université de Paris, CNRS, Paris, France , Paris (France)
  • 3 Centre de Recherche de Biologie cellulaire de Montpellier, UMR 5237, Université de Montpellier, CNRS, Montpellier, France , Montpellier (France)
  • 4 Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, MD, USA , Bethesda (United States)
  • 5 University of Minnesota, Minneapolis, MN, USA , Minneapolis (United States)
  • 6 Princess Margaret Cancer Centre, University Health Network, Toronto, ON, Canada , Toronto (Canada)
  • 7 Institut Gustave Roussy CNRS UMR9019, Villejuif, France , Villejuif (France)
  • 8 University of Toronto, Toronto, ON, Canada , Toronto (Canada)
Type
Published Article
Journal
Nature Communications
Publisher
Springer Nature
Publication Date
Mar 26, 2021
Volume
12
Issue
1
Identifiers
DOI: 10.1038/s41467-021-21922-w
Source
Springer Nature
License
Green

Abstract

Tavernier et al. decipher the mechanism by which the intrinsically disordered protein Bora, phosphorylated by Cyclin-Cdk, potentiates AURKA activity towards Polo-like kinase 1. Furthermore, they demonstrate the importance of this mechanism for timely mitotic entry in Xenopus and human cells.

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