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Plant J. 2012 Apr;70(2):348-56. doi: 10.1111/j.1365-313X.2011.04862.x. Epub 2012 Jan 10.

Identification of kinase substrates by bimolecular complementation assays.

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1
Unigruppe am Max-Planck-Institut für Züchtungsforschung, Max-Delbrück-Laboratorium, Lehrstuhl für Botanik III, Universität Köln, Carl-von-Linné-Weg 10, D-50829 Köln, Germany.

Abstract

As a consequence of the transient nature of kinase-substrate interactions, the detection of kinase targets, although central for understanding many biological processes, has remained challenging. Here we present a straightforward procedure that relies on the comparison of wild type with activation-loop mutants in the kinase of interest by bimolecular complementation assays. As a proof of functionality, we present the identification and in vivo confirmation of substrates of the major cell-cycle kinase in Arabidopsis, revealing a direct link between cell proliferation and the control of the redox state.

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