CDKB1;1 Forms a Functional Complex with CYCA2;3 to Suppress Endocycle Onset

被引:169
作者
Boudolf, Veronique [1 ,2 ]
Lammens, Tim [1 ,2 ]
Boruc, Joanna [1 ,2 ]
Van Leene, Jelle [1 ,2 ]
Van Den Daele, Hilde [1 ,2 ]
Maes, Sara [1 ,2 ]
Van Isterdael, Gert [1 ,2 ]
Russinova, Eugenia [1 ,2 ]
Kondorosi, Eva [3 ,4 ]
Witters, Erwin [5 ,6 ]
De Jaeger, Geert [1 ,2 ]
Inze, Dirk [1 ,2 ]
De Veylder, Lieven [1 ,2 ]
机构
[1] Univ Ghent VIB, Dept Plant Syst Biol, B-9052 Ghent, Belgium
[2] Univ Ghent, Dept Plant Biotechnol & Genet, B-9052 Ghent, Belgium
[3] CNRS, Inst Sci Vegetal, Unite Propre Rech 2355, F-91198 Gif Sur Yvette, France
[4] Bay Zoltan Fdn Appl Res, Inst Plant Genom Human Biotechnol & Bioenergy, H-6726 Szeged, Hungary
[5] Univ Antwerp, Ctr Proteome Anal & Mass Spectrometry, Dept Biol, B-2020 Antwerp, Belgium
[6] Flemish Inst Technol Res, B-2400 Mol, Belgium
关键词
ANAPHASE-PROMOTING COMPLEX; CYCLIN-DEPENDENT-KINASE; CELL-CYCLE; ARABIDOPSIS-THALIANA; TRANSCRIPTION FACTOR; FISSION YEAST; S-PHASE; PLANT DEVELOPMENT; DESTRUCTION BOX; ENDOREDUPLICATION;
D O I
10.1104/pp.109.140269
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The mitosis-to-endocycle transition requires the controlled inactivation of M phase-associated cyclin-dependent kinase (CDK) activity. Previously, the B-type CDKB1;1 was identified as an important negative regulator of endocycle onset. Here, we demonstrate that CDKB1;1 copurifies and associates with the A2-type cyclin CYCA2;3. Coexpression of CYCA2;3 with CDKB1;1 triggered ectopic cell divisions and inhibited endoreduplication. Moreover, the enhanced endoreduplication phenotype observed after overexpression of a dominant-negative allele of CDKB1;1 could be partially complemented by CYCA2;3 co-overexpression, illustrating that both subunits unite in vivo to form a functional complex. CYCA2;3 protein stability was found to be controlled by CCS52A1, an activator of the anaphase-promoting complex. We conclude that CCS52A1 participates in endocycle onset by down-regulating CDKB1;1 activity through the destruction of CYCA2;3.
引用
收藏
页码:1482 / 1493
页数:12
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