Drosophila Polo regulates the spindle assembly checkpoint through Mps1-dependent BubR1 phosphorylation

• Type: Article in International Scientific Journal
• Date: 2013

Authors

Conde, C (Author) Other; Osswald, M (Author) Other; Barbosa, J (Author) Other; Moutinho Santos, T (Author) Other; Pinheiro, D (Author) Other; Guimaraes, S (Author) Other; Matos, I (Author) Other; Helder Maiato (Author) FMUP; Sunkel, CE (Author) ICBAS

Journal

Title: EMBO Journal

Vol. 32

Pages: 1761-1777

ISSN: 0261-4189

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 35 Citations

Scopus - 34 Citations

Other information

Authenticus ID: P-005-01H

DOI: 10.1038/emboj.2013.109

Abstract (EN): Maintenance of genomic stability during eukaryotic cell division relies on the spindle assembly checkpoint (SAC) that prevents mitotic exit until all chromosomes are properly attached to the spindle. Polo is a mitotic kinase proposed to be involved in SAC function, but its role has remained elusive. We demonstrate that Polo and Aurora B functional interdependency comprises a positive feedback loop that promotes Mps1 kinetochore localization and activity. Expression of constitutively active Polo restores normal Mps1 kinetochore levels even after Aurora B inhibition, highlighting a role for Polo in Mps1 recruitment to unattached kinetochores downstream of Aurora B. We also show that Mps1 kinetochore localization is required for BubR1 hyperphosphorylation and formation of the 3F3/2 phosphoepitope. This is essential to allow recruitment of Cdc20 to unattached kinetochores and the assembly of anaphase-promoting complex/cyclosome-inhibitory complexes to levels that ensure long-term SAC activity. We propose a model in which Polo controls Mps1-dependent BubR1 phosphorylation to promote Cdc20 kinetochore recruitment and sustained SAC function.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 17