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

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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Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Q
Acceso en línea:https://doaj.org/article/c85f4e856295480db1bc7aa81205cfc6
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spelling oai:doaj.org-article:c85f4e856295480db1bc7aa81205cfc62021-12-02T14:02:51ZBora phosphorylation substitutes in trans for T-loop phosphorylation in Aurora A to promote mitotic entry10.1038/s41467-021-21922-w2041-1723https://doaj.org/article/c85f4e856295480db1bc7aa81205cfc62021-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21922-whttps://doaj.org/toc/2041-1723Tavernier 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.N. TavernierY. ThomasS. VigneronP. MaisonneuveS. OrlickyP. MaderS. G. RegmiL. Van HoveN. M. LevinsonG. Gasmi-SeabrookN. JolyM. PoteauG. Velez-AguileraO. GavetA. CastroM. DassoT. LorcaF. SicheriL. PintardNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-22 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
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.
format article
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
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 Portfolio
publishDate 2021
url https://doaj.org/article/c85f4e856295480db1bc7aa81205cfc6
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