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Vol. 10, Issue 11, 3909-3926, November 1999
and
*Max-Planck-Institut of Neurobiology and
Alternative pre-mRNA splicing patterns can change an extracellular
stimulus, but the signaling pathways leading to these changes are still
poorly characterized. Here, we describe a tyrosine-phosphorylated nuclear protein, YT521-B, and show that it interacts with the nuclear
transcriptosomal component scaffold attachment factor B, and the 68-kDa
Src substrate associated during mitosis, Sam68. Northern blot analysis
demonstrated ubiquitous expression, but detailed RNA in situ analysis
revealed cell type specificity in the brain. YT521-B protein is
localized in the nucleoplasm and concentrated in 5-20 large nuclear
dots. Deletion analysis demonstrated that the formation of these dots
depends on the presence of the amino-terminal glutamic acid-rich domain
and the carboxyl-terminal glutamic acid/arginine-rich region. We show
that the latter comprises an important protein-protein interaction
domain. The Src family kinase p59fyn-mediated tyrosine
phosphorylation of Sam68 negatively regulates its association with
YT521-B, and overexpression of p59fyn dissolves nuclear
dots containing YT521-B. In vivo splicing assays demonstrated that
YT521-B modulates alternative splice site selection in a
concentration-dependent manner. Together, our data indicate that
YT521-B and Sam68 may be part of a signal transduction pathway that
influences splice site selection.
Department of Molecular Biology, Max-Planck-Institut of
Biochemistry, D-82152 Martinsried, Germany
Corresponding author. E-mail address:
stamm{at}pop1.biochem.mpg.de.
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