ArticleScience advances2025
Structural assembly of maize CRY-GL2 photosignaling complex provides insights into its regulatory role in cuticular wax biosynthesis.
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- A CRY1 Interactor eIF3G1 Negatively Regulates Root Growth Under Blue Light inPlants (Basel, Switzerland) · 2026Article
- The Quantum Environment in Cryptochrome Enhances Light Absorption of FAD.bioRxiv : the preprint server for biology · 2026Article
- Blue-light-enhanced interaction between ZmCRY1s and GL2 modulates epidermal wax composition in Zea mays.Nature communications · 2025Article
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Authors and funding
12 authors.
Funding
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Abstract
Plant cryptochromes (CRYs) are blue-light photoreceptors regulating physiological processes via oligomerization-dependent interaction with effectors. However, the structural basis for photoactivated CRY-effector assembly remains elusive. Here, we report the crystal structure of an active maize CRY1c photolyase homology region in complex with GLOSSY2 (ZmGL2), a BAHD acyltransferase family protein that could form an enzyme complex with ECERIFERUM6 (ZmCER6) and direct very-long-chain fatty acid elongation in cuticular wax biosynthesis. Light-activated CRY1c forms a homotetrameric scaffold. Each protomer binds one ZmGL2 molecule via conformational changes, forming a 4:4 hetero-octameric photosignaling complex. Structural alignment shows 78% overlap between the GL2-binding interfaces in the ZmCRY1c-ZmGL2 and ZmCER6-ZmGL2 complexes. Biochemically, CRY1c dose-dependently inhibits ZmCER6-ZmGL2 enzyme activity, unveiling a light-dependent regulatory switch modulating very-long-chain fatty acid elongation efficiency. Our work establishes the atomic model for light-activated CRY-effector assembly and uncovers spatial competition between photoreceptor and metabolic enzyme complexes as a photoregulatory paradigm in wax biosynthesis.
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