SRPK1 and LBR protein kinases show identical substrate specificities.

@article{Papoutsopoulou1999SRPK1AL,
  title={SRPK1 and LBR protein kinases show identical substrate specificities.},
  author={Stamatia V. Papoutsopoulou and Eleni Nikolakaki and Thomas Giannakouros},
  journal={Biochemical and biophysical research communications},
  year={1999},
  volume={255 3},
  pages={602-7}
}
Arginine/serine protein kinases constitute a novel class of enzymes that can modify arginine/serine (RS) dipeptide motifs. SR splicing factors that are essential for pre-mRNA splicing and the lamin B receptor (LBR), an integral protein of the inner nuclear membrane, are among the best characterized proteins that contain RS domains. Two SR Protein-specific Kinases, SRPK1 and SRPK2, have been shown to phosphorylate specifically the RS motifs of the SR family of splicing factors and play an… CONTINUE READING

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