Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2024 Jun;242(6):2555-2569.
doi: 10.1111/nph.19742. Epub 2024 Apr 9.

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

Ting Li  1   2   3 , Yongqin Wang  1 , Annelore Natran  2   3 , Yi Zhang  1 , Hao Wang  4 , Kangxi Du  4 , Peng Qin  4 , Hua Yuan  1 , Weilan Chen  4 , Bin Tu  4 , Dirk Inzé #  2   3 , Marieke Dubois #  2   3
Affiliations

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

Ting Li et al. New Phytol. 2024 Jun.

Abstract

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

Keywords: Arabidopsis thaliana; C‐TERMINAL DOMAIN‐LIKE 3 (CPL3); DELLA; gibberellic acid; phosphatase; post‐translational regulation; protein degradation; protein dephosphorylation.

PubMed Disclaimer

Similar articles

See all similar articles

References

    1. Bang W, Kim S, Ueda A, Vikram M, Yun D, Bressan RA, Hasegawa PM, Bahk J, Koiwa H. 2006. Arabidopsis carboxyl‐terminal domain phosphatase‐like isoforms share common catalytic and interaction domains but have distinct in planta functions. Plant Physiology 142: 586–594.
    1. Blanco‐Touriñán N, Legris M, Minguet EG, Costigliolo‐Rojas C, Nohales MA, Iniesto E, García‐León M, Pacín M, Heucken N, Blomeier T et al. 2020a. COP1 destabilizes DELLA proteins in Arabidopsis. Proceedings of the National Academy of Sciences, USA 117: 13792–13799.
    1. Blanco‐Touriñán N, Serrano‐Mislata A, Alabadí D. 2020b. Regulation of DELLA proteins by post‐translational modifications. Plant & Cell Physiology 61: 1891–1901.
    1. Blázquez M. 2008. Phenotypic analysis of Arabidopsis mutants: gibberellin/abscisic acid/paclobutrazol hormone response. Cold Spring Harbor Protocols 2008: pdb.prot4964.
    1. Blom N, Gammeltoft S, Brunak S. 1999. Sequence and structure‐based prediction of eukaryotic protein phosphorylation sites. Journal of Molecular Biology 294: 1351–1362.

MeSH terms

LinkOut - more resources

-