Protein phosphatase-1 alpha, gamma 1, and delta: changes in phosphorylation and activity in mitotic HeLa cells and in cells released from the mitotic block.

@article{Puntoni1997ProteinPA,
  title={Protein phosphatase-1 alpha, gamma 1, and delta: changes in phosphorylation and activity in mitotic HeLa cells and in cells released from the mitotic block.},
  author={Franca Puntoni and Emma Villa-Moruzzi},
  journal={Archives of biochemistry and biophysics},
  year={1997},
  volume={340 2},
  pages={177-84}
}
Protein phosphatase-1 is phosphorylated "in vitro" by cdc2-cyclin B (E. Villa-Moruzzi, FEBS Lett. 304, 211-215, 1992). In the present study the phosphatase-1 isoforms alpha, gamma 1, and delta were analyzed in mitotic (nocodazole-blocked) HeLa cells. Phosphorylation on threonine increased in gamma 1 and delta at mitosis. alpha was phosphorylated only in mitotic cells and mainly on serine. Exposure of permeabilized mitotic cells to a peptide that inhibits cdc2 decreased the phosphorylation of… CONTINUE READING