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.

Bibliographic Details
Main Authors: 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
Format: Article
Language:English
Published: Nature Publishing Group 2021-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-21922-w
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spelling 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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