ArticlebioRxiv : the preprint server for biology2026
Bound for the nucleus: defining the molecular principles of cargo selection by importin 9.
Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Authors and funding
6 authors.
Funding
Abstract
Active nuclear transport of proteins enables essential nuclear processes, such as genome packaging, transcription, splicing, ribosome biogenesis, and DNA repair. To facilitate proper sorting between cytoplasmic and nuclear compartments, the importin class of chaperone proteins transports hundreds of proteins through hydrophobic nuclear pores. While some importins recognize cargos via classical nuclear localization signals (cNLSs), there is not a comprehensive understanding of binding specificity determinants for those that appear to recognize other cargo features. Here we subject one such importin, IPO9, which is known to import H2A-H2B, TFIIB, actin, and the proteasome into the nucleus without cNLS binding, to a detailed analysis of its full set of cargos and the structural elements of IPO9 that confer their recognition. Through cytoplasmic immunoprecipitation followed by mass spectrometry (IP-MS), we stringently and reproducibly identify 79
Identifiers
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Registered trials
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