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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2026,9,8]]},"abstract":"<jats:p>\n                    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\n                    <jats:italic toggle=\"yes\">Arabidopsis<\/jats:italic>\n                    DELLA protein REPRESSOR OF\n                    <jats:italic toggle=\"yes\">ga1-3<\/jats:italic>\n                    (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,\n                    <jats:italic toggle=\"yes\">cdk8<\/jats:italic>\n                    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\u2013coactivator interactions.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2619939123","type":"journal-article","created":{"date-parts":[[2026,8,31]],"date-time":"2026-08-31T19:03:24Z","timestamp":1788203004000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":0,"title":["CDK8 phosphorylation of DELLA limits Mediator recruitment in gibberellin signaling"],"prefix":"10.1073","volume":"123","author":[{"given":"Xu","family":"Huang","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00py81415","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology, Duke University","place":["Durham"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hongyi","family":"Chen","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00py81415","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology, Duke University","place":["Durham"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Larry","family":"Reser","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0153tk833","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Chemistry, University of Virginia","place":["Charlottesville"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8761-802X","authenticated-orcid":false,"given":"Andres V.","family":"Reyes","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/04jr01610","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology and Carnegie Mass Spectrometry Facility, Carnegie Institution for Science","place":["Stanford"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shou-Ling","family":"Xu","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/04jr01610","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology and Carnegie Mass Spectrometry Facility, Carnegie Institution for Science","place":["Stanford"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeffrey","family":"Shabanowitz","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0153tk833","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Chemistry, University of Virginia","place":["Charlottesville"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Donald F.","family":"Hunt","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0153tk833","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Chemistry, University of Virginia","place":["Charlottesville"]},{"id":[{"id":"https:\/\/ror.org\/0153tk833","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Pathology, University of Virginia","place":["Charlottesville"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5223-2936","authenticated-orcid":false,"given":"Tai-ping","family":"Sun","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00py81415","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology, Duke University","place":["Durham"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2026,8,31]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"publisher","DOI":"10.1002\/9781119210436.ch1"},{"key":"e_1_3_4_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature04028"},{"key":"e_1_3_4_3_2","doi-asserted-by":"publisher","DOI":"10.1093\/plphys\/kiae044"},{"key":"e_1_3_4_4_2","doi-asserted-by":"publisher","DOI":"10.1038\/22307"},{"key":"e_1_3_4_5_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev-arplant-053124-050732"},{"key":"e_1_3_4_6_2","doi-asserted-by":"publisher","DOI":"10.1105\/tpc.10.2.155"},{"key":"e_1_3_4_7_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.11.23.3194"},{"key":"e_1_3_4_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.semcdb.2020.04.009"},{"key":"e_1_3_4_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tplants.2017.07.010"},{"key":"e_1_3_4_10_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-313X.1999.00431.x"},{"key":"e_1_3_4_11_2","first-page":"1555","article-title":"Repressing a repressor: Gibberellin-induced rapid reduction of the RGA protein in Arabidopsis","volume":"13","author":"Silverstone A. 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