ArticleNature structural & molecular biology2020
Structural insights into BIC-mediated inactivation of Arabidopsis cryptochrome 2.
Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
33 citing papers in PubMed.
- Protocol to determine oligomerization states of proteins in living cells using photon counting histogram analysis.STAR protocols · 2026Article
- Time-Resolved Native Mass Spectrometry Reveals Reversible Light-Driven Oligomerization of Arabidopsis Cryptochrome 1 and Its Antagonism by BIC1.Angewandte Chemie (International ed. in English) · 2026Article
- The Quantum Environment in Cryptochrome Enhances Light Absorption of FAD.bioRxiv : the preprint server for biology · 2026Article
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Structural assembly of maize CRY-GL2 photosignaling complex provides insights into its regulatory role in cuticular wax biosynthesis.Science advances · 2025Article
- Resolving oligomeric states of photoactivatable proteins in living cells via photon counting histogram analysis.iScience · 2025Article
- Genome-Wide Identification and Characterization ofCurrent issues in molecular biology · 2025Article
- Light signaling in plants-a selective history.Plant physiology · 2024Review
- Timely Questions Emerging in Chronobiology: The Circadian Clock Keeps on Ticking.Journal of circadian rhythms · 2024Review
- Dual-transgenic BiFC vector systems for protein-protein interaction analysis in plants.Frontiers in genetics · 2024Article
- 'Seeing' the electromagnetic spectrum: spotlight on the cryptochrome photocycle.Frontiers in plant science · 2024Review
- A structural decryption of cryptochromes.Frontiers in chemistry · 2024Review
- Light-induced LLPS of the CRY2/SPA1/FIO1 complex regulating mRNA methylation and chlorophyll homeostasis in Arabidopsis.Nature plants · 2023Article
- BIC2, a Cryptochrome Function Inhibitor, Is Involved in the Regulation of ABA Responses inPlants (Basel, Switzerland) · 2023Article
- Cryo-EM structure of the CRY2 and CIB1 fragment complex provides insights into CIB1-mediated photosignaling.Plant communications · 2023Article
- RUP2 facilitates UVR8 redimerization via two interfaces.Plant communications · 2023Article
- Rapid and reversible optogenetic silencing of synaptic transmission by clustering of synaptic vesicles.Nature communications · 2022Article
- Direct experimental observation of blue-light-induced conformational change and intermolecular interactions of cryptochrome.Communications biology · 2022Article
- Optophysiology: Illuminating cell physiology with optogenetics.Physiological reviews · 2022Review
- Stop CRYing! Inhibition of cryptochrome function by small proteins.Biochemical Society transactions · 2022Review
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cryptochromes (CRYs) are blue-light receptors in plants that harbor FAD as a cofactor and regulate various physiological responses. Photoactivated CRYs undergo oligomerization, which increases the binding affinity to downstream signaling partners. Despite decades of research on the activation of CRYs, little is known about how they are inactivated. Binding of blue-light inhibitors of cryptochromes (BICs) to CRY2 suppresses its photoactivation, but the underlying mechanism remains unknown. Here, we report crystal structures of CRY2N (CRY2 PHR domain) and the BIC2-CRY2N complex with resolutions of 2.7 and 2.5 Å, respectively. In the BIC2-CRY2N complex, BIC2 exhibits an extremely extended structure that sinuously winds around CRY2N. In this way, BIC2 not only restrains the transfer of electrons and protons from CRY2 to FAD during photoreduction but also interacts with the CRY2 oligomer to return it to the monomer form. Uncovering the mechanism of CRY2 inactivation lays a solid foundation for the investigation of cryptochrome protein function.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.