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          Institute: MPI für molekulare Zellbiologie und Genetik     Collection: MPI-CBG Publications 2016 (archival)     Display Documents

ID: 732399.0, MPI für molekulare Zellbiologie und Genetik / MPI-CBG Publications 2016 (archival)
SR proteins are NXF1 adaptors that link alternative RNA processing to mRNA export.
Authors:Müller-McNicoll, Michaela; Botti, Valentina; Domingues, Antonio; Brandl, Holger; Schwich, Oliver D; Steiner, Michaela; Curk, Tomaz; Poser, Ina; Zarnack, Kathi; Neugebauer, Karla M.
Date of Publication (YYYY-MM-DD):2016
Title of Journal:Genes & Development
Issue / Number:5
Start Page:553
End Page:566
Copyright:not available
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:Nuclear export factor 1 (NXF1) exports mRNA to the cytoplasm after recruitment to mRNA by specific adaptor proteins. How and why cells use numerous different export adaptors is poorly understood. Here we critically evaluate members of the SR protein family (SRSF1-7) for their potential to act as NXF1 adaptors that couple pre-mRNA processing to mRNA export. Consistent with this proposal, >1000 endogenous mRNAs required individual SR proteins for nuclear export in vivo. To address the mechanism, transcriptome-wide RNA-binding profiles of NXF1 and SRSF1-7 were determined in parallel by individual-nucleotide-resolution UV cross-linking and immunoprecipitation (iCLIP). Quantitative comparisons of RNA-binding sites showed that NXF1 and SR proteins bind mRNA targets at adjacent sites, indicative of cobinding. SRSF3 emerged as the most potent NXF1 adaptor, conferring sequence specificity to RNA binding by NXF1 in last exons. Interestingly, SRSF3 and SRSF7 were shown to bind different sites in last exons and regulate 3' untranslated region length in an opposing manner. Both SRSF3 and SRSF7 promoted NXF1 recruitment to mRNA. Thus, SRSF3 and SRSF7 couple alternative splicing and polyadenylation to NXF1-mediated mRNA export, thereby controlling the cytoplasmic abundance of transcripts with alternative 3' ends.
External Publication Status:published
Document Type:Article
Version Comment:Automatic journal name synchronization
Communicated by:Thüm
Affiliations:MPI für molekulare Zellbiologie und Genetik
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