ArticlePLoS pathogens2026
FgNup2 regulates nuclear import of the histone H2B monoubiquitination enzyme by stabilizing the FgImpα-FgBre1 complex to mediate pathogenicity in Fusarium graminearum.
Article in PLoS pathogens, 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
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fusarium head blight caused by Fusarium graminearum threatens global wheat production. The pathogenicity of this fungus depends on histone H2B monoubiquitination (H2Bub1), yet the nuclear import mechanism of its key enzyme, FgBre1, remains unclear. In this study, we identified 24 nucleoporins in F. graminearum and found that FgNup2 is essential for fungal growth, toxin biosynthesis, and virulence. FgNup2 positively regulates H2Bub1 levels by facilitating the nuclear import of FgBre1, thereby influencing pathogenic development. The nuclear import of FgBre1 relies on the importin receptor FgImpα, and these two proteins interact. FgNup2, through a critical phenylalanine residue (F981) within its FG-repeat domain, promotes and stabilizes the FgImpα-FgBre1 complex, driving the assembly of the tripartite FgNup2-FgImpα-FgBre1 complex. This ultimately mediates the rapid nuclear translocation of FgBre1 under induction by the trichothecene biosynthesis-inducing medium. Our findings reveal a mechanism by which a nucleoporin regulates the nuclear entry of a histone-modifying enzyme via stabilizing the importin-cargo complex, advancing the understanding of non-canonical roles of the nuclear pore complex in pathogen adaptation.
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.