ArticleeLife2022
An amphipathic helix in Brl1 is required for nuclear pore complex biogenesis in
Article in eLife, 2022. 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, 25 citations in OpenAlex.
- Atg39-dependent nucleophagy and Atg40-dependent ER-phagy require the Apq12/Brr6/Brl1 complex.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A tool to pulse-label yeast nuclear pore complexes in imaging and biochemical experiments.eLife · 2026Article
- Screening of amphipathic helices identifies features linked to inner nuclear membrane properties.Nature communications · 2026Article
- Multifunctional roles of Brl1-Brr6 in nuclear envelope fusion during nuclear pore complex biogenesis.The EMBO journal · 2026Article
- Article
- RanBP2-dependent annulate lamellae drive nuclear pore assembly and nuclear expansion.Nature communications · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Elucidating the nanoscopic organization and dynamics of the nuclear pore complex.Nucleus (Austin, Tex.) · 2025Article
- Nuclear basket proteins regulate the distribution and mobility of nuclear pore complexes in budding yeast.Molecular biology of the cell · 2024Article
- Physical model of the nuclear membrane permeability mechanism.Biophysical reviews · 2023Review
- Lipid saturation controls nuclear envelope function.Nature cell biology · 2023Article
- Article
- Review
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Authors and funding
13 authors at 5 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear pore complex (NPC) is the central portal for macromolecular exchange between the nucleus and cytoplasm. In all eukaryotes, NPCs assemble into an intact nuclear envelope (NE) during interphase, but the process of NPC biogenesis remains poorly characterized. Furthermore, little is known about how NPC assembly leads to the fusion of the outer and inner NE, and no factors have been identified that could trigger this event. Here, we characterize the transmembrane protein Brl1 as an NPC assembly factor required for NE fusion in budding yeast. Brl1 preferentially associates with NPC assembly intermediates and its depletion halts NPC biogenesis, leading to NE herniations that contain inner and outer ring nucleoporins but lack the cytoplasmic export platform. Furthermore, we identify an essential amphipathic helix in the luminal domain of Brl1 that mediates interactions with lipid bilayers. Mutations in this amphipathic helix lead to NPC assembly defects, and cryo-electron tomography analyses reveal multilayered herniations of the inner nuclear membrane with NPC-like structures at the neck, indicating a failure in NE fusion. Taken together, our results identify a role for Brl1 in NPC assembly and suggest a function of its amphipathic helix in mediating the fusion of the inner and outer nuclear membranes.
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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.