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

Joanna Boruc, Annika Weimer, Virginie Stoppin-Mellet, Evelien Mylle UGent, Ken Kosetsu UGent, Cesyen Cedeño, Michel Jaquinod, Maria Njo UGent, Liesbeth De Milde UGent, Peter Tompa, et al. (2017) PLANT PHYSIOLOGY. 173(1). p.582-599
abstract
Aurora kinases are key effectors of mitosis. Plant Auroras are functionally divided into two clades. The alpha Auroras (Aurora1 and Aurora2) associate with the spindle and the cell plate and are implicated in controlling formative divisions throughout plant development. The beta 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 homolog 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, yeasts, and plants-is a genuine substrate of alpha Aurora kinases. MAP65-1 interacts with Aurora1 in vivo and is phosphorylated on two residues at its unfolded tail domain. Its overexpression and down-regulation antagonistically affect the alpha 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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
MICROTUBULE-ASSOCIATED PROTEINS, CAENORHABDITIS-ELEGANS EMBRYOS, DNA-DAMAGE RESPONSE, SPINDLE MIDZONE, RETINOBLASTOMA PROTEIN, GLYCOGEN-SYNTHASE, BUDDING YEAST, HISTONE H3, IN-VITRO, CYTOKINESIS
journal title
PLANT PHYSIOLOGY
Plant Physiol.
volume
173
issue
1
pages
582 - 599
Web of Science type
Article
Web of Science id
000394135800043
ISSN
0032-0889
1532-2548
DOI
10.1104/pp.16.01602
project
Biotechnology for a sustainable economy (Bio-Economy)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have retained and own the full copyright for this publication
id
8516850
handle
http://hdl.handle.net/1854/LU-8516850
date created
2017-04-04 10:08:50
date last changed
2017-07-03 10:16:45
@article{8516850,
  abstract     = {Aurora kinases are key effectors of mitosis. Plant Auroras are functionally divided into two clades. The alpha Auroras (Aurora1 and Aurora2) associate with the spindle and the cell plate and are implicated in controlling formative divisions throughout plant development. The beta 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 homolog 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, yeasts, and plants-is a genuine substrate of alpha Aurora kinases. MAP65-1 interacts with Aurora1 in vivo and is phosphorylated on two residues at its unfolded tail domain. Its overexpression and down-regulation antagonistically affect the alpha 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.},
  author       = {Boruc, Joanna and Weimer, Annika and Stoppin-Mellet, Virginie and Mylle, Evelien and Kosetsu, Ken and Cede{\~n}o, Cesyen and Jaquinod, Michel and Njo, Maria and De Milde, Liesbeth and Tompa, Peter and Gonzalez Sanchez, Nathalie and Inz{\'e}, Dirk and Beeckman, Tom and Vantard, Marylin and Van Damme, Dani{\"e}l},
  issn         = {0032-0889},
  journal      = {PLANT PHYSIOLOGY},
  keyword      = {MICROTUBULE-ASSOCIATED PROTEINS,CAENORHABDITIS-ELEGANS EMBRYOS,DNA-DAMAGE RESPONSE,SPINDLE MIDZONE,RETINOBLASTOMA PROTEIN,GLYCOGEN-SYNTHASE,BUDDING YEAST,HISTONE H3,IN-VITRO,CYTOKINESIS},
  language     = {eng},
  number       = {1},
  pages        = {582--599},
  title        = {Phosphorylation of MAP65-1 by Arabidopsis Aurora kinases is required for efficient cell cycle progression},
  url          = {http://dx.doi.org/10.1104/pp.16.01602},
  volume       = {173},
  year         = {2017},
}

Chicago
Boruc, Joanna, Annika Weimer, Virginie Stoppin-Mellet, Evelien Mylle, Ken Kosetsu, Cesyen Cedeño, Michel Jaquinod, et al. 2017. “Phosphorylation of MAP65-1 by Arabidopsis Aurora Kinases Is Required for Efficient Cell Cycle Progression.” Plant Physiology 173 (1): 582–599.
APA
Boruc, J., Weimer, A., Stoppin-Mellet, V., Mylle, E., Kosetsu, K., Cedeño, C., Jaquinod, M., et al. (2017). Phosphorylation of MAP65-1 by Arabidopsis Aurora kinases is required for efficient cell cycle progression. PLANT PHYSIOLOGY, 173(1), 582–599.
Vancouver
1.
Boruc J, Weimer A, Stoppin-Mellet V, Mylle E, Kosetsu K, Cedeño C, et al. Phosphorylation of MAP65-1 by Arabidopsis Aurora kinases is required for efficient cell cycle progression. PLANT PHYSIOLOGY. 2017;173(1):582–99.
MLA
Boruc, Joanna, Annika Weimer, Virginie Stoppin-Mellet, et al. “Phosphorylation of MAP65-1 by Arabidopsis Aurora Kinases Is Required for Efficient Cell Cycle Progression.” PLANT PHYSIOLOGY 173.1 (2017): 582–599. Print.