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TitleImportin-9 recognizes the winged-helix fold of ETS transcription factors to mediate nuclear import.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 123, Issue 18, Page e2536763123, Year 2026
Publish dateMay 5, 2026
AuthorsMichael McConville / Kaylee Lankford / Natalia E Bernardes / Abby Walterscheid / Catherine Valadez / Ashley Niesman / Yuh Min Chook / Glen Liszczak /
PubMed AbstractProtein trafficking between the cytoplasm and the nucleus is a fundamental process in eukaryotic cell biology. While linear nuclear localization signals (NLSs) are well characterized, many nuclear ...Protein trafficking between the cytoplasm and the nucleus is a fundamental process in eukaryotic cell biology. While linear nuclear localization signals (NLSs) are well characterized, many nuclear proteins lack a predictable NLS. Here, we identify the ETS domain, a DNA-binding winged-helix fold, from ETS family transcription factors as a structure-encoded NLS. We show that ETS domains mediate nuclear import through direct nanomolar affinity recognition by IPO9. Cryo-electron microscopy analysis of the EHF:IPO9 complex reveals that the IPO9 wraps around the ETS domain and engages structural features throughout the winged-helix fold. Biochemical studies demonstrate that the ETS domain DNA-binding helix is critical for importin recognition and for NLS activity in mammalian cells. Comparison of IPO9 bound to EHF and the histone H2A:H2B dimer reveals distinct interaction hotspots, illustrating how IPO9 employs unique combinatorial binding surfaces to accommodate structurally diverse cargos. These findings define a unique class of globular NLSs and highlight the adaptability of importins in recognizing distinct protein folds.
External linksProc Natl Acad Sci U S A / PubMed:42066049 / PubMed Central
MethodsEM (single particle)
Resolution3.5 Å
Structure data

75437

10sm

EMDB-75437, PDB-10sm:
Importin-9 bound to ETS homologous factor (EHF)
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • homo sapiens (human)
KeywordsNUCLEAR PROTEIN / Nuclear Import / Importin / DNA-binding protein / winged-helix domain

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