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The STAR/GSG family protein rSLM-2 regulates the selection of alternative splice sites.

We identified the rat Sam68-like mammalian protein (rSLM-2), a member of the STAR (signal transduction and activation of RNA) protein family as a novel splicing regulatory protein. Using the yeast two-hybrid system, coimmunoprecipitations, and pull-down assays, we demonstrate that rSLM-2 interacts with various proteins involved in the regulation of alternative splicing, among them the serine/arginine-rich protein SRp30c, the splicing-associated factor YT521-B and the scaffold attachment factor B. rSLM-2 can influence the splicing pattern of the CD44v5, human transformer-2beta and tau minigenes in cotransfection experiments. This effect can be reversed by rSLM-2-interacting proteins. Employing rSLM-2 deletion variants, gel mobility shift assays, and linker scan mutations of the CD44 minigene, we show that the rSLM-2-dependent inclusion of exon v5 of the CD44 pre-mRNA is dependent on a short purine-rich sequence. Because the related protein of rSLM-2, Sam68, is believed to play a role as an adapter protein during signal transduction, we postulate that rSLM-2 is a link between signal transduction pathways and pre-mRNA processing.

Pubmed ID: 11118435


  • Stoss O
  • Olbrich M
  • Hartmann AM
  • Konig H
  • Memmott J
  • Andreadis A
  • Stamm S


The Journal of biological chemistry

Publication Data

March 23, 2001

Associated Grants

  • Agency: NINDS NIH HHS, Id: R01 NS38051

Mesh Terms

  • Alternative Splicing
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Line
  • Cloning, Molecular
  • DNA, Complementary
  • Enhancer Elements, Genetic
  • Exons
  • Humans
  • Molecular Sequence Data
  • RNA-Binding Proteins
  • Recombinant Proteins
  • Saccharomyces cerevisiae
  • Two-Hybrid System Techniques