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. 2017 Apr 10;8:502. doi: 10.3389/fpls.2017.00502

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Copyright © 2017 Lyzenga, Sullivan, Liu and Stone.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Calcineurin B-like interacting protein kinase 26 (CIPK26) can phosphorylate KEG in vitro and active CIPK26 promotes the proteasome-dependent turnover of KEG in a cell free degradation assay. (A) In vitro phosphorylation assays using Flag-His-KEGRK and Flag-His-CIPK26N, Flag-His-CIPK26N^KR (inactive) or Flag-His-CIPK26N^TD (constitutively active). Autoradiogram shows self-phosphorylation of CIPK26N and phosphorylation of KEG by CIPK26N and CIPK26N^TD. Autoradiogram is representative of two trials. (B) Modified cell free degradation assay in which purified Flag-His-CIPK26N^TD or Flag-His-CIPK26N^KR was added to protein extracts prepared from 6-day-old 35S:HA-KEG seedlings. HA-KEG protein levels were determined by western blotting (WB) using HA antibodies at the indicated time points. (C) Quantification of two trials using signal intensity at each time point determined by IMAGEJ. The error bar represents ± standard error.