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Structural basis for the synergistic assembly of the snRNA export complex
Open accessPreprint — published as 10.1038/s41594-025-01595-5 · Paper page
Abstract
The nuclear cap-binding complex (CBC) and its partner ARS2 play crucial roles in regulating Pol II transcript fate through mutually exclusive interactions with RNA effectors. One such effector, PHAX, mediates the nuclear export of U-rich small nuclear RNAs (snRNAs). Here we present the cryo-EM structure of the snRNA export complex comprising phosphorylated PHAX, CBC, CRM1, Ran-GTP and capped RNA. The central region of PHAX bridges the CBC-bound capped RNA to the CRM1-RanGTP, while also significantly reinforcing cap dinucleotide binding. Additionally, PHAX interacts with a distant region of CRM1 facilitating contacts of an essential phosphorylated region with the prominent basic surface of RanGTP. The importance of these interactions is confirmed by in vitro and in cell mutagenesis experiments. CBC engagement within the snRNA export complex is incompatible with its interactions with other RNA effectors such as ALYREF or NCBP3. Taken together, we demonstrate that snRNA export complex formation requires synergistic binding of all its components, which in turn displaces ARS2 from the CBC, and commits the complex for export.
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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Dubiez, E., Garland, W., Brask, M. F., Erba, E. B., Jensen, T. H., Kadlec, J., & Cusack, S.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Aarhus University (DK)
- European Molecular Biology Laboratory (FR)
- Corresponding author
- Kadlec, Jan
- Cusack, Stephen
- ORCID
- Venue
- Nature Structural & Molecular Biology
- Publisher
- openRxiv
- Published
- 2024-11-28
- Volume
- 32
- Issue
- 8
- Pages
- 1555-1566
- ISSN
- 1545-9985 (ISSN-L)
- PMC
- PMC12350170
- OpenAlex
- W4412008164
- Cited by
- 9
- References
- 1
- Citations by year
- 2026: 7 · 2025: 2
- FWCI
- 2.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Nature Structural & Molecular Biology (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- European Molecular Biology Laboratory (UAR 3518 CNRS-CEA-UGA-EMBL)
- Agence Nationale de la Recherche (UAR 3518 CNRS-CEA-UGA-EMBL, ANR-24-CE11-4977, ANR-17-EURE-0003, ANR-17-EURE-, ANR-21-CE11-0021, ANR-17, ANR-10, ANR-10-INBS-0005)
- Novo Nordisk
- Centre National de la Recherche Scientifique (ANR‐17‐EURE‐0003, UAR 3518 CNRS-CEA-UGA-EMBL)
- French Infrastructure for Integrated Structural Biology (UAR 3518 CNRS-CEA-UGA-EMBL, ANR-17-EURE-0003, ANR-10-INBS-0005, ANR-10-INBS-000502, ANR-10-INBS)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- nuclear cap-binding complex, ARS2, small nuclear RNA, RNA export, RNA-protein interactions, RNA polymerase II transcripts, ALYREF, protein complex structure
- MeSH terms
- Exportin 1 Protein, Humans, Models, Molecular, Nuclear Proteins, Phosphoproteins, Phosphorylation, Protein Binding, RNA, Small Nuclear, RNA-Binding Proteins, Receptors, Cytoplasmic and Nuclear, Cryoelectron Microscopy, ran GTP-Binding Protein, Active Transport, Cell Nucleus, Karyopherins, Nucleocytoplasmic Transport Proteins, Nuclear Cap-Binding Protein Complex
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