P59fyn-mediated phosphorylation regulates the activity of the tissue-specific splicing factor rSLM-1

Oliver Stoss, Tatyana Novoyatleva, Marieta Gencheva, Manuela Olbrich, Natalya Benderska, Stefan Stamm

Research output: Contribution to journalArticlepeer-review

45 Scopus citations


The Sam68-like mammalian protein SLM-1 is a member of the STAR protein family and is related to SAM68 and SLM-2. Here, we demonstrate that rSLM-1 interacts with itself, scaffold-attachment factor B, YT521-B, SAM68, rSLM-2, SRp30c, and hnRNP G. rSLM-1 regulates splice site selection in vivo via a purine-rich enhancer. In contrast to the widely expressed SAM68 and rSLM-2 proteins, rSLM-1 is found primarily in brain and, to a much smaller degree, in testis. In the brain, rSLM-1 and rSLM-2 are predominantly expressed in different neurons. In the hippocampal formation, rSLM-1 is present only in the dentate gyrus, whereas rSLM-2 is found in the pyramidal cells of the CA1, CA3, and CA4 regions. rSLM-1, but not rSLM-2, is phosphorylated by p59fyn. p59fyn-mediated phosphorylation abolishes the ability of rSLM-1 to regulate splice site selection, but has no effect on rSLM-2 activity. This suggests that rSLM-1-positive cells could respond with a change of their splicing pattern to p59fyn activation, whereas rSLM-2-positive cells would not be affected. Together, our data indicate that rSLM-1 is a tissue-specific splicing factor whose activity is regulated by tyrosine phosphorylation signals emanating from p59fyn.

Original languageEnglish
Pages (from-to)8-21
Number of pages14
JournalMolecular and Cellular Neuroscience
Issue number1
StatePublished - Sep 2004

Bibliographical note

Funding Information:
This work was supported by the Deutsche Forschungsgemeinschaft (DFG) to SS. We thank Gregor Eichele for help with microscopy.


  • 3-amino-triazole
  • 3′ UTR
  • 3′ untranslated region
  • 4,6 Diamidino-2-phenylindole
  • AT
  • DAPI
  • EGFP
  • EST
  • KH domain
  • PBS
  • enhanced green fluorescent protein
  • expressed sequence tag
  • hnRNP K homology domain
  • htra2-beta
  • human transformer-2-beta

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience
  • Cell Biology


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