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      Interplays between auxin and GA signaling coordinate early fruit development

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      Horticulture Research
      Oxford University Press

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          Abstract

          Phytohormones and their interactions are critical for fruit development and are key topics in horticulture research. Auxin, together with gibberellic acid (GA), promotes cell division and expansion, thereby regulating fruit development and enlargement after fertilization. Auxin- and GA-related mutants show parthenocarpy (fruit formation without fertilization of the ovule) in many plant species, indicating that these hormones and possibly their interactions play a key role in the regulation of fruit initiation and development. Recent studies have shown clear molecular and genetic evidence that ARF/IAA and DELLA proteins interact with one another and regulate both auxin and GA signaling pathways in response to auxin and GA during fruit growth in horticultural plants such as tomato (the most studied fleshy fruit) and strawberry (the model for Rosaceae). These recent findings provide new insights into the mechanisms by which the plant hormones auxin and GA regulate fruit development.

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          Most cited references91

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          GIBBERELLIN INSENSITIVE DWARF1 encodes a soluble receptor for gibberellin.

          Gibberellins (GAs) are phytohormones that are essential for many developmental processes in plants. It has been postulated that plants have both membrane-bound and soluble GA receptors; however, no GA receptors have yet been identified. Here we report the isolation and characterization of a new GA-insensitive dwarf mutant of rice, gid1. The GID1 gene encodes an unknown protein with similarity to the hormone-sensitive lipases, and we observed preferential localization of a GID1-green fluorescent protein (GFP) signal in nuclei. Recombinant glutathione S-transferase (GST)-GID1 had a high affinity only for biologically active GAs, whereas mutated GST-GID1 corresponding to three gid1 alleles had no GA-binding affinity. The dissociation constant for GA4 was estimated to be around 10(-7) M, enough to account for the GA dependency of shoot elongation. Moreover, GID1 bound to SLR1, a rice DELLA protein, in a GA-dependent manner in yeast cells. GID1 overexpression resulted in a GA-hypersensitive phenotype. Together, our results indicate that GID1 is a soluble receptor mediating GA signalling in rice.
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            DELLAs modulate jasmonate signaling via competitive binding to JAZs.

            Gibberellins (GAs) modulate jasmonate (JA) signaling, which is essential for stress response and development in plants. However, the molecular details of such phytohormone interaction remain largely unknown. Here, we show that the JA ZIM-domain 1 (JAZ1) protein, a key repressor of JA signaling, interacts in vivo with DELLA proteins, repressors of the GA pathway. DELLAs prevent inhibitory JAZ1 interaction with a key transcriptional activator of JA responses, MYC2, and, thus, enhance the ability of MYC2 to regulate its target genes. Conversely, GA triggers degradation of DELLAs, which allows JAZ1 to bind MYC2 and suppress MYC2-dependent JA-signaling outputs. Therefore, our results reveal one means by which GAs suppress cellular competence to respond to JA. Because DELLAs serve as central regulators that mediate the crosstalk of various phytohormones, our model also suggests a candidate mechanism by which JA signaling may be fine-tuned by other signaling pathways through DELLAs. Copyright © 2010 Elsevier Inc. All rights reserved.
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              Gibberellin-induced DELLA recognition by the gibberellin receptor GID1.

              Gibberellins control a range of growth and developmental processes in higher plants and have been widely used in the agricultural industry. By binding to a nuclear receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), gibberellins regulate gene expression by promoting degradation of the transcriptional regulator DELLA proteins, including GIBBERELLIN INSENSITIVE (GAI). The precise manner in which GID1 discriminates and becomes activated by bioactive gibberellins for specific binding to DELLA proteins remains unclear. Here we present the crystal structure of a ternary complex of Arabidopsis thaliana GID1A, a bioactive gibberellin and the amino-terminal DELLA domain of GAI. In this complex, GID1A occludes gibberellin in a deep binding pocket covered by its N-terminal helical switch region, which in turn interacts with the DELLA domain containing DELLA, VHYNP and LExLE motifs. Our results establish a structural model of a plant hormone receptor that is distinct from the mechanism of the hormone perception and effector recognition of the known auxin receptors.
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                Author and article information

                Contributors
                Journal
                Hortic Res
                Hortic Res
                hr
                Horticulture Research
                Oxford University Press
                2662-6810
                2052-7276
                2022
                19 January 2022
                19 January 2022
                : 9
                : uhab078
                Affiliations
                FAFU-UCR Joint Center for Horticultural Biology and Metabolomics, Haixia Institute of Science and Technology, Fujian Agriculture and Forestry University , Fuzhou 350002, Fujian, China
                FAFU-UCR Joint Center for Horticultural Biology and Metabolomics, Haixia Institute of Science and Technology, Fujian Agriculture and Forestry University , Fuzhou 350002, Fujian, China
                Author notes
                Corresponding author. E-mail: c.yamamuro@ 123456fafu.edu.cn
                Article
                uhab078
                10.1093/hr/uhab078
                8955447
                35043212
                6cb02f54-8bda-4bce-8650-5e14bec637a1
                © The Author(s) 2022. Published by Oxford University Press on behalf of Nanjing Agricultural University

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 16 August 2021
                : 2 November 2021
                : 23 March 2022
                Page count
                Pages: 09
                Categories
                Review Article

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