Phosphorylation of MAP65-1 by Arabidopsis Aurora kinases is required for efficient cell cycle progression.

TitlePhosphorylation of MAP65-1 by Arabidopsis Aurora kinases is required for efficient cell cycle progression.
Publication TypeJournal Article
Year of Publication2016
AuthorsBoruc, J., Weimer A., Stoppin-Mellet V., Mylle E., Kosetsu K., Cedeño C., Jaquinod M., Njo M., De Milde L., Tompa P., Gonzalez N., Inzé D., Beeckman T., Vantard M., and van Damme D.
JournalPlant Physiol
Date Published2016 Nov 22
ISSN1532-2548
Abstract

Aurora kinases are key effectors of mitosis. Plant Auroras are functionally divided into two clades. The α Auroras (Aurora1 and Aurora2) associate with the spindle and the cell plate and are implicated in controlling formative divisions throughout plant development. The β Aurora (Aurora3) localizes to centromeres and likely functions in chromosome separation. In contrast to the wealth of data available on the role of Aurora in other kingdoms, knowledge on their function in plants is merely emerging. This is exemplified by the fact that only histone H3 and the plant homologue of TPX2 have been identified as Aurora substrates in plants. Here we provide biochemical, genetic and cell biological evidence that the microtubule-bundling protein MAP65-1, a member of the MAP65/Ase1/PRC1 protein family, implicated in central spindle formation and cytokinesis in animals, yeast and plants, is a genuine substrate of α Aurora kinases. MAP65-1 interacts with Aurora1 in vivo and is phosphorylated on two residues at its unfolded tail domain. Its over-expression and down-regulation antagonistically affect the α Aurora double mutant phenotypes. Phospho-mutant analysis shows that Aurora contributes to the microtubule bundling capacity of MAP65-1 in concert with other mitotic kinases.

DOI10.1104/pp.16.01602
Alternate JournalPlant Physiol.
PubMed ID27879390
Research group: