ArticleThe New phytologist2026
The GSK3/SHAGGY-like OsGSK3 phosphorylates and inhibits phase separation of OsFCA at Ser-43 and Ser-45 to regulate brassinosteroid signaling and rice architecture.
Article in The New phytologist, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors.
Funding
Abstract
Brassinosteroid (BR) signaling plays a critical role in rice (Oryza sativa L.) grain development. GLYCOGEN SYNTHASE KINASE 3 (OsGSK3), a negative regulator of BR signaling, suppresses the transcriptional activity of OsBZR1 through phosphorylation. In this study, we employed a phosphoproteomic approach to construct an OsGSK3-mediated regulatory network. Within this network, we identified FLOWERING CONTROL LOCUS A (OsFCA) as a positive regulator of BR signaling and grain length, with m-Osfca mutants exhibiting significantly lower sensitivity to brassinolide treatment. Importantly, OsGSK3 interacts with and phosphorylates OsFCA on serine residues S43 and S45, and then forms condensates via liquid-liquid phase separation. Phosphorylated OsFCA promotes the translocation of the OsGSK3-OsFCA complex into the cytoplasm. Within the cytoplasm, OsGSK3 and OsFCA no longer exist in a condensate state. This mechanism provides precise regulation of grain length in rice. Notably, Osfca mutants are late-flowering, with OsFCA promoting heading under long-day conditions by repressing the expression of Grain number, plant height and heading date 7 (Ghd7) while activating that of Early heading date 1 (Ehd1), Heading date 3a (Hd3a), and RICE FLOWERING LOCUS T 1 (RFT1), which is potentially modulated by OsGSK3. This study clarifies the BR signaling transduction network by identifying OsFCA as a positive BR signaling component that regulates grain development and heading date, providing theoretical foundations for molecular breeding design in rice.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.