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Molecular basis for blue light-dependent phosphorylation of Arabidopsis CRY2 has been described.
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The results demonstrate a CRY-BIC negative-feedback circuitry that regulates the activity of each other.
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Verticillium dahliae PevD1 indirectly activates Arabidopsis CRY2 by antagonizing NRP functions. The promotion of CRY2-mediated flowering by a fungal effector outlines a novel pathway by which an external stimulus is recognized and transferred in changing a developmental program.
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CRY2-CIB1 and CRY2-CRY2 interactions are governed by well-separated protein interfaces at the two termini of CRY2.
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Exposure to blue light is required for an in vivo-association of CRY1 and CRY2 with COP1.
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Data show that the effect of 3-bromo-7-nitroindazole (3B7N) treatment on gene expression in cryptochromes cry1cry2 is considerably smaller than that in the wild type, indicating that 3B7N specifically interrupts cryptochrome function in the control of seedling development in a light-dependent manner.
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It describes minimal functional CRY2 and CIB1 domains maintaining light-dependent interaction and new signaling mutations affecting Arabidopsis thaliana cryptochrome 2 (AtCRY2) photocycle kinetics.
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this study identified BIC1 (blue-light inhibitor of cryptochromes 1) as an inhibitor of plant cryptochromes that binds to CRY2 to suppress the blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
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the blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele (axr6-3), especially under the non-permissive temperature.
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For growth under a canopy, where blue light is diminished, CRY1 and CRY2 perceive this change and respond by directly contacting two bHLH transcription factors, PIF4 and PIF5.
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Arabidopsis thaliana cry2 proteins containing Trp triad mutations indeed undergo robust photoreduction in living cultured insect cells.
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data showed that mutations in the serine residues within and outside the serine cluster diminished blue light-dependent CRY2 phosphorylation, degradation, and physiological activities.
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Our study demonstrates that CIBs function redundantly in regulating CRY2-dependent flowering, and that different CIBs form heterodimers to interact with the non-canonical E-box DNA in vivo.
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Studies show that CK1.3 (At4g28880) and CK1.4 (At4g28860) directly phosphorylate CRY2 at Ser-587 and Thr-603 in vitro and negatively regulate CRY2 stability, which are stimulated by blue light.
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Based on the loss of degradation of cry2 after prolonged darkness and loss of reversibility of photoactivated cry1 by a pulse of green light, we estimate the in vivo half-lives of the signaling states of cry1 and cry2 to be in the range of 5 and 16 min.
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Data indicate that although cryptochrome 2 physically interacts with CIB1 in response to blue light, ZEITLUPE and LOV KELCH PROTEIN 2 are required for the function and blue-light suppression of degradation of CIB1.
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fusing AtCRY2 to the TopBP1 DNA damage checkpoint protein, light-induced AtCRY2 PBs can be used to activate DNA damage signaling pathway in the absence of DNA damage
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Data indicate that the green light (GL) opposition of red light (RL) responses persists in phyA, phyB, cry1cry2 and phot2 mutants, and the response requires phot1 and NPH3.
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Degradation of Arabidopsis CRY2 is regulated by SPA1, Spa2, Spa4 proteins and phytochrome A.
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The photoexcited cryptochromes form oligomers, preceding other biochemical changes of CRY2, facilitate photobody formation, signal amplification, and propagation, as well as desensitization by degradation.
