C‐TERMINAL DOMAIN PHOSPHATASE‐LIKE 3 contributes to GA‐mediated growth and flowering by interaction with DELLA proteins

• DOI: 10.1111/nph.19742
• Publication Date: 2024-04-10T02:25:36Z
• Authors: Ting Li; Yongqin Wang; Annelore Natran; Yi Zhang; Hao Wang; Kangxi Du; Peng Qin; Hua Yuan; Weilan Chen; Bin Tu; Dirk Inzé; Marieke Dubois
• Keywords: Dephosphorylation; F-box protein

Summary Gibberellic acid (GA) plays a central role in many plant developmental processes and is crucial for crop improvement. DELLA proteins, the core suppressors GA signaling pathway, are degraded by via 26S proteasomal pathway to release response. However, little known about phosphorylation‐mediated regulation of proteins. In this study, we combined response assays with protein–protein interaction analysis infer connection between Arabidopsis thaliana DELLAs C‐TERMINAL DOMAIN PHOSPHATASE‐LIKE 3 (CPL3), phosphatase involved dephosphorylation RNA polymerase II. We show that CPL3 directly interacts proteins promotes protein stability inhibiting its degradation proteasome. Consequently, negatively modulates multiple GA‐mediated development, including hypocotyl elongation, flowering time, anthocyanin accumulation. Taken together, our findings demonstrate serves as novel regulator could improve thereby participate transduction.