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Updated: Sep 2, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
CDK8 phosphorylation of DELLA limits Mediator recruitment in gibberellin signaling
Xu Huang1, Hongyi Chen1, Larry Reser2
1Department of Biology, Duke University, Durham, NC 27708.
Abstract:
Gibberellin (GA) promotes plant growth primarily by triggering degradation of DELLA transcription regulators, yet how DELLA activity is fine-tuned dynamically by phosphorylation independently of proteolysis remains poorly understood. Here, we show that the CDK8 kinase module of the Mediator complex attenuates activity of the Arabidopsis DELLA protein REPRESSOR OF ga1-3 (RGA) by modulating coactivator recruitment. Using TurboID-based proximity labeling, biochemical and genetic analyses, we identify CDK8 as an in planta kinase that phosphorylates RGA at Ser170 within its disordered PolyS/T region. This phosphorylation does not affect RGA stability, localization, or interactions with transcription factors or histone H2A, but selectively weakens RGA association with the Mediator subunit MED15, thereby reducing DELLA-dependent transcription activation. Consistently, cdk8 mutants show impaired GA-responses and delayed developmental phase transitions that are partially rescued by loss of DELLA function. Our findings uncover a phosphorylation-dependent mechanism by which the Mediator kinase module fine-tunes hormone-responsive transcription through selective control of DELLA-coactivator interactions.
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