ArticleInternational journal of molecular sciences2014
14-3-3 proteins participate in light signaling through association with PHYTOCHROME INTERACTING FACTORs.
Article in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- 14-3-3 proteins: Central hubs in plant development and stress adaptation.Journal of integrative plant biology · 2026Review
- The phytochrome B signaling regulates salt-mediated seedling growth in the dark.Plant & cell physiology · 2025Article
- Review
- Haplotype Analysis of GmSGF14 Gene Family Reveals Its Roles in Photoperiodic Flowering and Regional Adaptation of Soybean.International journal of molecular sciences · 2023Article
- Identification of the 14-3-3 Gene Family in Bamboo and Characterization ofInternational journal of molecular sciences · 2022Article
- The role of 14-3-3 proteins in plant growth and response to abiotic stress.Plant cell reports · 2022Review
- Genome-wide identification of the 14-3-3 gene family and its participation in floral transition by interacting with TFL1/FT in apple.BMC genomics · 2021Article
- Light Modulates Ethylene Synthesis, Signaling, and Downstream Transcriptional Networks to Control Plant Development.Frontiers in plant science · 2019Review
- Shade-induced nuclear localization of PIF7 is regulated by phosphorylation and 14-3-3 proteins ineLife · 2018Article
- Dormancy in Embryos: Insight from Hydrated Encysted Embryos of an Aquatic Invertebrate.Molecular & cellular proteomics : MCP · 2017Article
- Holophytochrome-Interacting Proteins in Physcomitrella: Putative Actors in Phytochrome Cytoplasmic Signaling.Frontiers in plant science · 2016Article
- A 14-3-3 Family Protein from Wild Soybean (Glycine Soja) Regulates ABA Sensitivity in Arabidopsis.PloS one · 2015Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
14-3-3 proteins are regulatory proteins found in all eukaryotes and are known to selectively interact with phosphorylated proteins to regulate physiological processes. Through an affinity purification screening, many light-related proteins were recovered as 14-3-3 candidate binding partners. Yeast two-hybrid analysis revealed that the 14-3-3 kappa isoform (14-3-3κ) could bind to PHYTOCHROME INTERACTING FACTOR3 (PIF3) and CONSTITUTIVE PHOTOMORPHOGENIC1 (COP1). Further analysis by in vitro pull-down assay confirmed the interaction between 14-3-3κ and PIF3. Interruption of putative phosphorylation sites on the 14-3-3 binding motifs of PIF3 was not sufficient to inhibit 14-3-3κ from binding or to disturb nuclear localization of PIF3. It was also indicated that 14-3-3κ could bind to other members of the PIF family, such as PIF1 and PIF6, but not to LONG HYPOCOTYL IN FAR-RED1 (HFR1). 14-3-3 mutants, as well as the PIF3 overexpressor, displayed longer hypocotyls, and a pif3 mutant displayed shorter hypocotyls than the wild-type in red light, suggesting that 14-3-3 proteins are positive regulators of photomorphogenesis and function antagonistically with PIF3. Consequently, our results indicate that 14-3-3 proteins bind to PIFs and initiate photomorphogenesis in response to a light signal.
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