Bora phosphorylation substitutes in trans for T-loop phosphorylation in Aurora A to promote mitotic entry
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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2021-03-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-021-21922-w |
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doaj-c85f4e856295480db1bc7aa81205cfc62021-03-28T11:13:03ZengNature Publishing GroupNature Communications2041-17232021-03-0112112210.1038/s41467-021-21922-wBora phosphorylation substitutes in trans for T-loop phosphorylation in Aurora A to promote mitotic entryN. Tavernier0Y. Thomas1S. Vigneron2P. Maisonneuve3S. Orlicky4P. Mader5S. G. Regmi6L. Van Hove7N. M. Levinson8G. Gasmi-Seabrook9N. Joly10M. Poteau11G. Velez-Aguilera12O. Gavet13A. Castro14M. Dasso15T. Lorca16F. Sicheri17L. Pintard18Centre for Systems Biology, Lunenfeld Tanenbaum Research Institute, Sinai Health SystemProgramme équipe Labellisée Ligue Contre le Cancer, Institut Jacques Monod, UMR7592, Université de Paris, CNRSCentre de Recherche de Biologie cellulaire de Montpellier, UMR 5237, Université de Montpellier, CNRSCentre for Systems Biology, Lunenfeld Tanenbaum Research Institute, Sinai Health SystemCentre for Systems Biology, Lunenfeld Tanenbaum Research Institute, Sinai Health SystemCentre for Systems Biology, Lunenfeld Tanenbaum Research Institute, Sinai Health SystemEunice Kennedy Shriver National Institute of Child Health and Human DevelopmentProgramme équipe Labellisée Ligue Contre le Cancer, Institut Jacques Monod, UMR7592, Université de Paris, CNRSDepartment of Pharmacology, University of MinnesotaPrincess Margaret Cancer Centre, University Health NetworkProgramme équipe Labellisée Ligue Contre le Cancer, Institut Jacques Monod, UMR7592, Université de Paris, CNRSInstitut Gustave Roussy CNRS UMR9019Programme équipe Labellisée Ligue Contre le Cancer, Institut Jacques Monod, UMR7592, Université de Paris, CNRSInstitut Gustave Roussy CNRS UMR9019Centre de Recherche de Biologie cellulaire de Montpellier, UMR 5237, Université de Montpellier, CNRSEunice Kennedy Shriver National Institute of Child Health and Human DevelopmentCentre de Recherche de Biologie cellulaire de Montpellier, UMR 5237, Université de Montpellier, CNRSCentre for Systems Biology, Lunenfeld Tanenbaum Research Institute, Sinai Health SystemProgramme équipe Labellisée Ligue Contre le Cancer, Institut Jacques Monod, UMR7592, Université de Paris, CNRSTavernier 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.https://doi.org/10.1038/s41467-021-21922-w |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
N. Tavernier Y. Thomas S. Vigneron P. Maisonneuve S. Orlicky P. Mader S. G. Regmi L. Van Hove N. M. Levinson G. Gasmi-Seabrook N. Joly M. Poteau G. Velez-Aguilera O. Gavet A. Castro M. Dasso T. Lorca F. Sicheri L. Pintard |
spellingShingle |
N. Tavernier Y. Thomas S. Vigneron P. Maisonneuve S. Orlicky P. Mader S. G. Regmi L. Van Hove N. M. Levinson G. Gasmi-Seabrook N. Joly M. Poteau G. Velez-Aguilera O. Gavet A. Castro M. Dasso T. Lorca F. Sicheri L. Pintard Bora phosphorylation substitutes in trans for T-loop phosphorylation in Aurora A to promote mitotic entry Nature Communications |
author_facet |
N. Tavernier Y. Thomas S. Vigneron P. Maisonneuve S. Orlicky P. Mader S. G. Regmi L. Van Hove N. M. Levinson G. Gasmi-Seabrook N. Joly M. Poteau G. Velez-Aguilera O. Gavet A. Castro M. Dasso T. Lorca F. Sicheri L. Pintard |
author_sort |
N. Tavernier |
title |
Bora phosphorylation substitutes in trans for T-loop phosphorylation in Aurora A to promote mitotic entry |
title_short |
Bora phosphorylation substitutes in trans for T-loop phosphorylation in Aurora A to promote mitotic entry |
title_full |
Bora phosphorylation substitutes in trans for T-loop phosphorylation in Aurora A to promote mitotic entry |
title_fullStr |
Bora phosphorylation substitutes in trans for T-loop phosphorylation in Aurora A to promote mitotic entry |
title_full_unstemmed |
Bora phosphorylation substitutes in trans for T-loop phosphorylation in Aurora A to promote mitotic entry |
title_sort |
bora phosphorylation substitutes in trans for t-loop phosphorylation in aurora a to promote mitotic entry |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2021-03-01 |
description |
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. |
url |
https://doi.org/10.1038/s41467-021-21922-w |
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