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

IF 8.1 1区生物学 Q1 PLANT SCIENCES New Phytologist Pub Date : 2024-04-09 DOI:10.1111/nph.19742

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

引用次数: 0

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C-TERMINAL DOMAIN PHOSPHATASE-LIKE 3 通过与 DELLA 蛋白相互作用，为 GA 介导的生长和开花做出贡献

摘要赤霉素（GA）在许多植物发育过程中起着核心作用，对作物改良至关重要。DELLA蛋白是GA信号通路中的核心抑制因子，可通过26S蛋白酶体途径被GA降解，从而释放GA反应。然而，人们对磷酸化介导的 DELLA 蛋白调控知之甚少。在这项研究中，我们结合了 GA 响应测定和蛋白-蛋白相互作用分析，推断拟南芥 DELLA 与 C-TERMINAL DOMAIN PHOSPHATASE-LIKE 3（CPL3）之间的联系，C-TERMINAL DOMAIN PHOSPHATASE-LIKE 3 是一种参与 RNA 聚合酶 II 去磷酸化的磷酸酶。我们的研究表明，CPL3 直接与 DELLA 蛋白相互作用，并通过抑制 26S 蛋白酶体的降解来促进 DELLA 蛋白的稳定性。因此，CPL3 对植物发育过程中由 GA 介导的多个过程（包括下胚轴伸长、开花时间和花青素积累）具有负向调节作用。综上所述，我们的研究结果表明 CPL3 是一种新型调控因子，可提高 DELLA 的稳定性，从而参与 GA 信号转导。

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来源期刊

New Phytologist 生物-植物科学

自引率

5.30%

发文量

728

期刊介绍： New Phytologist is an international electronic journal published 24 times a year. It is owned by the New Phytologist Foundation, a non-profit-making charitable organization dedicated to promoting plant science. The journal publishes excellent, novel, rigorous, and timely research and scholarship in plant science and its applications. The articles cover topics in five sections: Physiology & Development, Environment, Interaction, Evolution, and Transformative Plant Biotechnology. These sections encompass intracellular processes, global environmental change, and encourage cross-disciplinary approaches. The journal recognizes the use of techniques from molecular and cell biology, functional genomics, modeling, and system-based approaches in plant science. Abstracting and Indexing Information for New Phytologist includes Academic Search, AgBiotech News & Information, Agroforestry Abstracts, Biochemistry & Biophysics Citation Index, Botanical Pesticides, CAB Abstracts®, Environment Index, Global Health, and Plant Breeding Abstracts, and others.