ArticleMolecular cell2025
Exportin-1 functions as an adaptor for transcription factor-mediated docking of chromatin at the nuclear pore complex.
Article in Molecular cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Targeting Exportin-1 in Cancer: From Nuclear Export to Oncogenic Transcriptional Hubs.JMA journal · 2026Review
- Beyond nuclear export: chromatin-bound XPO1/CRM1 as a transcriptional scaffold.International journal of hematology · 2026Review
- Karyopherin Dysfunction Is a Key Driver of Aging.Aging cell · 2026Review
- Silencing lipid catabolism determines longevity in response to fasting.Nature communications · 2026Article
- Review
- The nuclear export receptor CRM1/XPO1 and its diverse cargoes.Trends in biochemical sciences · 2025Review
- Review
- Article
- Nuclear basket proteins Nup2 and Mlp1 drive heat shock-induced 3D genome restructuring downstream of transcriptional activation.The Journal of biological chemistry · 2025Article
- Nuclear basket proteins Nup2 and Mlp1 drive heat shock-induced 3D genome restructuring downstream of transcriptional activation.bioRxiv : the preprint server for biology · 2025Article
- Isoform differences drive functional diversity of NHR-49.microPublication biology · 2025Article
- Chromatin endogenous cleavage provides a global view of yeast RNA polymerase II transcription kinetics.eLife · 2024Article
- Chromatin endogenous cleavage provides a global view of yeast RNA polymerase II transcription kinetics.bioRxiv : the preprint server for biology · 2024Article
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14 authors.
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Abstract
Nuclear pore proteins (nucleoporins [Nups]) physically interact with hundreds of chromosomal sites, impacting transcription. In yeast, transcription factors mediate interactions between Nups and enhancers and promoters. To define the molecular basis of this mechanism, we exploited a separation-of-function mutation in the Gcn4 transcription factor that blocks its interaction with the nuclear pore complex (NPC). This mutation reduces the interaction of Gcn4 with the highly conserved nuclear export factor Crm1/Xpo1. Crm1 and Nups co-occupy enhancers, and Crm1 inhibition blocks interaction of the nuclear pore protein Nup2 with the genome. In vivo, Crm1 interacts stably with the NPC and in vitro, Crm1 binds directly to both Gcn4 and Nup2. Importantly, the interaction between Crm1 and Gcn4 requires neither Ran-guanosine triphosphate (GTP) nor the nuclear export sequence binding site. Finally, Crm1 and Ran-GTP stimulate DNA binding by Gcn4, suggesting that allosteric coupling between Crm1-Ran-GTP binding and DNA binding facilitates the docking of transcription-factor-bound enhancers at the NPC.
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Registered trials
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