A novel splicing regulator shares a nuclear import pathway with SR proteins

EMBO J. 2003 Mar 17;22(6):1359-69. doi: 10.1093/emboj/cdg126.

Abstract

Alternative splicing of precursor mRNA is often regulated by serine/arginine-rich proteins (SR proteins) and hnRNPs, and varying their concentration in the nucleus can be a mechanism for controlling splice site selection. To understand the nucleocytoplasmic transport mechanism of splicing regulators is of key importance. SR proteins are delivered to the nucleus by transportin-SRs (TRN-SRs), importin beta-like nuclear transporters. Here we identify and characterize a non-SR protein, RNA-binding motif protein 4 (RBM4), as a novel substrate of TRN-SR2. TRN-SR2 interacts specifically with RBM4 in a Ran-sensitive manner. TRN-SR2 indeed mediates the nuclear import of a recombinant protein containing the RBM4 C-terminal domain. This domain serves as a signal for both nuclear import and export, and for nuclear speckle targeting. Finally, both in vivo and in vitro splicing analyses demonstrate that RBM4 not only modulates alternative pre-mRNA splicing but also acts antagonistically to authentic SR proteins in splice site and exon selection. Thus, a novel splicing regulator with opposite activities to SR proteins shares an identical import pathway with SR proteins to the nucleus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus
  • Amino Acid Sequence
  • Aspartate Carbamoyltransferase / metabolism
  • Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) / metabolism
  • Cell Nucleus / metabolism
  • Dihydroorotase / metabolism
  • Exons
  • Genes, Insect
  • HeLa Cells
  • Humans
  • Molecular Sequence Data
  • Multienzyme Complexes / metabolism
  • Nerve Growth Factors
  • Nuclear Localization Signals
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Phosphoproteins / metabolism
  • Protein Structure, Tertiary
  • Proteins / metabolism
  • RNA Precursors / metabolism
  • RNA Splice Sites
  • RNA Splicing*
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Serine / metabolism
  • Substrate Specificity
  • Two-Hybrid System Techniques
  • beta Karyopherins / metabolism

Substances

  • CAD trifunctional enzyme
  • MANF protein, human
  • Multienzyme Complexes
  • Nerve Growth Factors
  • Nuclear Localization Signals
  • Nuclear Proteins
  • Phosphoproteins
  • Proteins
  • RBM4 protein, human
  • RNA Precursors
  • RNA Splice Sites
  • RNA-Binding Proteins
  • Recombinant Proteins
  • beta Karyopherins
  • transportin SR2
  • Serine
  • Aspartate Carbamoyltransferase
  • Dihydroorotase
  • Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)