Coupling of Polo kinase activation to nuclear localization by a bifunctional NLS is required during mitotic entry

David Kachaner, Damien Garrido, Haytham Mehsen, Karine Normandin, Hugo Lavoie and Vincent Archambault ()
Additional contact information
David Kachaner: Institute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128 Succursale Centre-Ville
Damien Garrido: Institute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128 Succursale Centre-Ville
Haytham Mehsen: Institute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128 Succursale Centre-Ville
Karine Normandin: Institute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128 Succursale Centre-Ville
Hugo Lavoie: Institute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128 Succursale Centre-Ville
Vincent Archambault: Institute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128 Succursale Centre-Ville

Nature Communications, 2017, vol. 8, issue 1, 1-16

Abstract: Abstract The Polo kinase is a master regulator of mitosis and cytokinesis conserved from yeasts to humans. Polo is composed of an N-term kinase domain (KD) and a C-term polo-box domain (PBD), which regulates its subcellular localizations. The PBD and KD can interact and inhibit each other, and this reciprocal inhibition is relieved when Polo is phosphorylated at its activation loop. How Polo activation and localization are coupled during mitotic entry is unknown. Here we report that PBD binding to the KD masks a nuclear localization signal (NLS). Activating phosphorylation of the KD leads to exposure of the NLS and entry of Polo into the nucleus before nuclear envelope breakdown. Failures of this mechanism result in misregulation of the Cdk1-activating Cdc25 phosphatase and lead to mitotic and developmental defects in Drosophila. These results uncover spatiotemporal mechanisms linking master regulatory enzymes during mitotic entry.

Date: 2017
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-017-01876-8 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01876-8

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-017-01876-8

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().