p59 super(f) super(y) super(n)-mediated phosphorylation regulates the activity of the tissue-specific splicing factor rSLM-1

• Published in: Molecular and cellular neuroscience 2004-09, Vol.27 (1), p.8-21
• Main Authors: Stoss, O, Novoyatleva, T, Gencheva, M, Olbrich, M, Benderska, N, Stamm, S
• Format: Article
• Language: English
• ISSN: 1044-7431
• DOI: 10.1016/j.mcn.2004.04.011

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 p59 super(f) super(y) super(n). p59 super(f) super(y) super(n)-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 p59 super(f) super(y) super(n) 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 p59 super(f) super(y) super(n).