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  A multi-factor trafficking site on the spliceosome remodeling enzyme BRR2 recruits C9ORF78 to regulate alternative splicing

Bergfort, A., Preußner, M., Kuropka, B., Ilik, I. A., Hilal, T., Weber, G., et al. (2022). A multi-factor trafficking site on the spliceosome remodeling enzyme BRR2 recruits C9ORF78 to regulate alternative splicing. Nature Communications, 13: 1132 (2022). doi:10.1038/s41467-022-28754-2.

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NatureComm_Bergfort et al_2022.pdf (Publisher version), 6MB
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Bergfort, Alexandra , Author
Preußner, Marco , Author
Kuropka, Benno , Author
Ilik, Ibrahim Avsar1, Author              
Hilal, Tarek , Author
Weber, Gert, Author
Freund, Christian, Author
Aktas, Tugce1, Author              
Heyd, Florian , Author
Wahl, Markus C. , Author
Affiliations:
1Quantitative RNA Biology (Tugce Aktas), Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_3014184              

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 Abstract: The intrinsically unstructured C9ORF78 protein was detected in spliceosomes but its role in splicing is presently unclear. We find that C9ORF78 tightly interacts with the spliceosome remodeling factor, BRR2, in vitro. Affinity purification/mass spectrometry and RNA UV-crosslinking analyses identify additional C9ORF78 interactors in spliceosomes. Cryogenic electron microscopy structures reveal how C9ORF78 and the spliceosomal B complex protein, FBP21, wrap around the C-terminal helicase cassette of BRR2 in a mutually exclusive manner. Knock-down of C9ORF78 leads to alternative NAGNAG 3′-splice site usage and exon skipping, the latter dependent on BRR2. Inspection of spliceosome structures shows that C9ORF78 could contact several detected spliceosome interactors when bound to BRR2, including the suggested 3′-splice site regulating helicase, PRPF22. Together, our data establish C9ORF78 as a late-stage splicing regulatory protein that takes advantage of a multi-factor trafficking site on BRR2, providing one explanation for suggested roles of BRR2 during splicing catalysis and alternative splicing.

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Language(s): eng - English
 Dates: 2022-02-102022-03-03
 Publication Status: Published online
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 Rev. Type: -
 Identifiers: DOI: 10.1038/s41467-022-28754-2
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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 13 Sequence Number: 1132 (2022) Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723