Splicing factor SRp30c interaction with Y-box protein-1 confers nuclear YB-1 shuttling and alternative splice site selection.

@article{Raffetseder2003SplicingFS,
  title={Splicing factor SRp30c interaction with Y-box protein-1 confers nuclear YB-1 shuttling and alternative splice site selection.},
  author={Ute Raffetseder and Bj{\"o}rn Christian Frye and Thomas Rauen and Karsten Juerchott and H Royer and Petra Lynen Jansen and Peter R. Mertens},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 20},
  pages={18241-8}
}
The multifunctional DNA- and RNA-associated Y-box protein 1 (YB-1) specifically binds to splicing recognition motifs and regulates alternative splice site selection. Here, we identify the arginine/serine-rich SRp30c protein as an interacting protein of YB-1 by performing a two-hybrid screen against a human mesangial cell cDNA library. Co-immunoprecipitation studies confirm a direct interaction of tagged proteins YB-1 and SRp30c in the absence of RNA via two independent protein domains of YB-1… CONTINUE READING
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