The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9.

@article{Lavoie2001ThePI,
  title={The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9.},
  author={S{\'e}bastien B. Lavoie and Alexandra Albert and Hiroshi Handa and M. Vincent and Olivier Bensaude},
  journal={Journal of molecular biology},
  year={2001},
  volume={312 4},
  pages={675-85}
}
We identify and characterize several phosphorylated forms of the hSpt5 subunit of the DRB sensitivity-inducing factor (DSIF). A 175-kDa phosphorylated form of hSpt5 is bound to nuclei of interphase HeLa cells. This form is rapidly dephosphorylated when cultured cells are exposed to various drugs belonging to distinct chemical families. All these compounds are known to inhibit the protein kinase Cdk9, which phosphorylates in vitro hSpt5 and Rpb1, the largest subunit of RNA polymerase II. The… CONTINUE READING