2026-10-13T19:09:52Z
https://api.figshare.com/v2/oai
oai:figshare.com:article/33814660
2026-09-15T18:00:22Z
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category_272
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portal_5
item_type_3
month_year_09_2026
<p>Raw data.</p>
Yaxuan Wang (4670974)
Zhe Li (219258)
Xiaoyan Wang (8433)
Bin Xiong (445687)
Chengqi Zhang (116222)
Xiaozhen Zhao (4579963)
Shentao Wang (24950245)
Li Chen (5749)
Biochemistry
Space Science
Medicine
Microbiology
Cell Biology
Genetics
Molecular Biology
Environmental Sciences not elsewhere classified
Biological Sciences not elsewhere classified
Plant Biology
two proteins interact
identified 24 nucleoporins
h2bub1 ), yet
div >< p
critical phenylalanine residue
rapid nuclear translocation
fusarium graminearum </
nuclear pore complex
importin receptor fgimpα
histone h2b monoubiquitination
nuclear import mechanism
graminearum </
nuclear import
nuclear entry
ultimately mediates
trichothecene biosynthesis
toxin biosynthesis
repeat domain
remains unclear
nucleoporin regulates
key enzyme
inducing medium
fungus depends
fungal growth
findings reveal
fgnup2 </
canonical roles
<div><p>Fusarium head blight caused by <i>Fusarium graminearum</i> 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 <i>F. graminearum</i> and found that <i>FgNup2</i> 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.</p></div>
2026-09-15T18:00:31Z
Dataset
Dataset
10.1371/journal.ppat.1014577.s002
https://figshare.com/articles/dataset/_p_Raw_data_p_/33814660
CC BY 4.0