Identification of kinase substrates by bimolecular complementation assays
2012
Pusch, Stefan | Harashima, Hirofumi | Schnittger, Arp
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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