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

Author:

Boudolf Véronique1,Lammens Tim1,Boruc Joanna1,Van Leene Jelle1,Van Den Daele Hilde1,Maes Sara1,Van Isterdael Gert1,Russinova Eugenia1,Kondorosi Eva1,Witters Erwin1,De Jaeger Geert1,Inzé Dirk1,De Veylder Lieven1

Affiliation:

1. Department of Plant Systems Biology, Flanders Institute for Biotechnology, 9052 Ghent, Belgium (V.B., T.L., J.B., J.V.L., H.V.D.D., S.M., G.V.I., E.R., G.D.J., D.I., L.D.V.); Department of Plant Biotechnology and Genetics, Ghent University, 9052 Ghent, Belgium (V.B., T.L., J.B., J.V.L., H.V.D.D., S.M., G.V.I., E.R., G.D.J., D.I., L.D.V.); Institut des Sciences du Végétal, Centre National de la

Abstract

AbstractThe 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.

Publisher

Oxford University Press (OUP)

Subject

Plant Science,Genetics,Physiology

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