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KMID : 0368420160590060627
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Journal of Plant Biology
2016 Volume.59 No. 6 p.627 ~ p.638
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WDRP, a DWD protein component of CUL4-based E3 ligases, acts as a receptor of CDPK-related protein kinase 5 to mediate kinase degradation in Arabidopsis
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Teng Hui-Juan
Guo Yue
Wang Jian-Qi
Li Rongjun
Lu Ying-Tang
Zhang Lei
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Abstract
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CRK5 is a member of the Arabidopsis thaliana Ca2+-dependent protein kinase-related kinase family. Here, a yeast two-hybrid screen was performed with a truncated form of AtCRK5 as bait to identify interacting proteins and determine its physiological roles. One gene encoding the DWD protein WDRP was isolated. Furthermore, in vitro and in vivo co-immunoprecipitation results strongly supported that these two proteins interact with each other. Using a cell-free degradation assay, we also established that CRK5 was an unstable protein that was degraded through the proteasome pathway. The rate of CRK5 degradation was delayed in a WDRP knockout line. On the other hand, the degradation of CRK5 mediated by WDRP might not affect the phosphorylation of PIN2 by CRK5. Overall, we demonstrated that AtCRK5 interacted with a DWD protein, AtWDRP; the protein AtWDRP targets the kinase for ubiquitin-dependent degradation. Therefore, this report describes a new kinase regulation pathway for CRK family proteins in Arabidopsis.
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KEYWORD
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Ca2+-dependent protein kinase-related kinases (CRKs), CUL4-based E3 ligase, DDB1 binding WD40 box (DWD box) Ubiquitin, WD40
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