ArticlePLoS genetics2017
The blue light-induced interaction of cryptochrome 1 with COP1 requires SPA proteins during Arabidopsis light signaling.
Article in PLoS genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 67 citations in OpenAlex.
- Mineral nutrients as regulators of plant flowering time: A molecular perspective.Journal of integrative plant biology · 2026Review
- Deciphering Protein Interaction Dynamics Using the Yeast Three-Hybrid System.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Cryptochrome 1 promotes photomorphogenesis in Arabidopsis by displacing substrates from the COP1 ubiquitin ligase.The Plant journal : for cell and molecular biology · 2025Article
- CONSTANS, a HUB for all seasons: How photoperiod pervades plant physiology regulatory circuits.The Plant cell · 2024Review
- Light signaling in plants-a selective history.Plant physiology · 2024Review
- Diurnal Rhythms in the Red Seaweed Gracilariopsis chorda are Characterized by Unique Regulatory Networks of Carbon Metabolism.Molecular biology and evolution · 2024Article
- The mechanism of low blue light-induced leaf senescence mediated by GmCRY1s in soybean.Nature communications · 2024Article
- Photoperiodic flowering in Arabidopsis: Multilayered regulatory mechanisms of CONSTANS and the florigen FLOWERING LOCUS T.Plant communications · 2023Review
- Shade avoidance in the context of climate change.Plant physiology · 2023Article
- The blue light signal transduction module FaCRY1-FaCOP1-FaHY5 regulates anthocyanin accumulation in cultivated strawberry.Frontiers in plant science · 2023Article
- UBP12 and UBP13 deubiquitinases destabilize the CRY2 blue light receptor to regulate Arabidopsis growth.Current biology : CB · 2022Article
- Article
- Divergence of flowering-related genes to control flowering in five Euphorbiaceae genomes.Frontiers in plant science · 2022Article
- Signaling Mechanisms by Arabidopsis Cryptochromes.Frontiers in plant science · 2022Review
- Arabidopsis cryptochrome 1 controls photomorphogenesis through regulation of H2A.Z deposition.The Plant cell · 2021Article
- Perception of solar UV radiation by plants: photoreceptors and mechanisms.Plant physiology · 2021Article
- The involvement of theaBIOTECH · 2021Review
- Regulation of Arabidopsis photoreceptor CRY2 by two distinct E3 ubiquitin ligases.Nature communications · 2021Article
- Illuminating the COP1/SPA Ubiquitin Ligase: Fresh Insights Into Its Structure and Functions During Plant Photomorphogenesis.Frontiers in plant science · 2021Review
- Low Blue Light Enhances Phototropism by Releasing Cryptochrome1-Mediated Inhibition ofPlant physiology · 2020Article
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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
Plants constantly adjust their growth, development and metabolism to the ambient light environment. Blue light is sensed by the Arabidopsis photoreceptors CRY1 and CRY2 which subsequently initiate light signal transduction by repressing the COP1/SPA E3 ubiquitin ligase. While the interaction between cryptochromes and SPA is blue light-dependent, it was proposed that CRY1 interacts with COP1 constitutively, i.e. also in darkness. Here, our in vivo co-immunoprecipitation experiments suggest that CRY1 and CRY2 form a complex with COP1 only after seedlings were exposed to blue light. No association between COP1 and CRY1 or CRY2 was observed in dark-grown seedlings. Thus, our results suggest that cryptochromes bind the COP1/SPA complex after photoactivation by blue light. In a spa quadruple mutant that is devoid of all four SPA proteins, CRY1 and COP1 did not interact in vivo, neither in dark-grown nor in blue light-grown seedlings. Hence, SPA proteins are required for the high-affinity interaction between CRY1 and COP1 in blue light. Yeast three-hybrid experiments also show that SPA1 enhances the CRY1-COP1 interaction. The coiled-coil domain of SPA1 which is responsible for COP1-binding was necessary to mediate a CRY1-SPA1 interaction in vivo, implying that-in turn-COP1 may be necessary for a CRY1-SPA1 complex formation. Hence, SPA1 and COP1 may act cooperatively in recognizing and binding photoactivated CRY1. In contrast, the blue light-induced association between CRY2 and COP1 was not dependent on SPA proteins in vivo. Similarly, ΔCC-SPA1 interacted with CRY2, though with a much lower affinity than wild-type SPA1. In total, our results demonstrate that CRY1 and CRY2 strongly differ in their blue light-induced interaction with the COP1/SPA complex.
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