Abstract
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 language | English |
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Pages (from-to) | 8-21 |
Number of pages | 14 |
Journal | Molecular and Cellular Neuroscience |
Volume | 27 |
Issue number | 1 |
DOIs | |
State | Published - 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.
Keywords
- 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