SAP30BP interacts with RBM17/SPF45 to promote splicing in a subset of human short introns

Kazuhiro Fukumura, Luca Sperotto, Stefanie Seuß, Hyun Seo Kang, Rei Yoshimoto, Michael Sattler, Akila Mayeda

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Human pre-mRNA splicing requires the removal of introns with highly variable lengths, from tens to over a million nucleotides. Therefore, mechanisms of intron recognition and splicing are likely not universal. Recently, we reported that splicing in a subset of human short introns with truncated polypyrimidine tracts depends on RBM17 (SPF45), instead of the canonical splicing factor U2 auxiliary factor (U2AF) heterodimer. Here, we demonstrate that SAP30BP, a factor previously implicated in transcriptional control, is an essential splicing cofactor for RBM17. In vitro binding and nuclear magnetic resonance analyses demonstrate that a U2AF-homology motif (UHM) in RBM17 binds directly to a newly identified UHM-ligand motif in SAP30BP. We show that this RBM17-SAP30BP interaction is required to specifically recruit RBM17 to phosphorylated SF3B1 (SF3b155), a U2 small nuclear ribonucleoprotein (U2 snRNP) component in active spliceosomes. We propose a mechanism for splicing in a subset of short introns, in which SAP30BP guides RBM17 in the assembly of active spliceosomes.

Original languageEnglish
Article number113534
JournalCell Reports
Volume42
Issue number12
DOIs
StatePublished - 26 Dec 2023
Externally publishedYes

Keywords

  • CP: Molecular biology
  • RBM17
  • SAB30BP
  • SF3B1
  • SF3b155
  • SPF45
  • U2 snRNP
  • U2AF heterodimer
  • U2AF-homology motif
  • UHM
  • UHM-ligand motif
  • ULM
  • polypyrimidine tract
  • pre-mRNA splicing
  • short intron

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