Interaction of protein phosphatase type 1 with a splicing factor

Katsuya Hirano, Ferenc Erdödi, James G. Patton, David J. Hartshorne

Research output: Contribution to journalArticle

59 Citations (Scopus)


A gizzard cDNA library was screened by the two-hybrid system using as bait the δ isoform of the catalytic subunit of protein phosphatase 1 (PP1δ). Among the proteins identified was a fragment of the polypyrimidine tract-binding protein-associated splicing factor (PSF) and for 242 residues was 97.1% identical to the human isoforms. Binding of PSP and PP1δ was confirmed by inhibition of phosphatase activity and by an overlay technique. The PP1δ binding site was contained in the N-terminal 82 residues of the PSF fragment, PSP may therefore act as a PP1 target molecule in the spliceosome.

Original languageEnglish
Pages (from-to)191-194
Number of pages4
JournalFEBS letters
Issue number2
Publication statusPublished - Jul 1 1996



  • Human splicing factor PSF
  • Protein phosphatase type 1
  • Two-hybrid system

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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