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Identification of kinase substrates by bimolecular complementation assays
Author(s) -
Pusch Stefan,
Harashima Hirofumi,
Schnittger Arp
Publication year - 2012
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/j.1365-313x.2011.04862.x
Subject(s) - identification (biology) , complementation , protein fragment complementation assay , computational biology , kinase , bimolecular fluorescence complementation , chemistry , microbiology and biotechnology , biology , biochemistry , gene , phenotype , botany
Summary 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.