PP1-mediated dephosphorylation of phosphoproteins at mitotic exit is controlled by inhibitor-1 and PP1 phosphorylation

Nat Cell Biol. 2009 May;11(5):644-51. doi: 10.1038/ncb1871. Epub 2009 Apr 26.

Abstract

Loss of cell division cycle 2 (Cdc2, also known as Cdk1) activity after cyclin B degradation is necessary, but not sufficient, for mitotic exit. Proteins phosphorylated by Cdc2 and downstream mitotic kinases must be dephosphorylated. We report here that protein phosphatase-1 (PP1) is the main catalyst of mitotic phosphoprotein dephosphorylation. Suppression of PP1 during early mitosis is maintained through dual inhibition by Cdc2 phosphorylation and the binding of inhibitor-1. Protein kinase A (PKA) phosphorylates inhibitor-1, mediating binding to PP1. As Cdc2 levels drop after cyclin B degradation, auto-dephosphorylation of PP1 at its Cdc2 phosphorylation site (Thr 320) allows partial PP1 activation. This promotes PP1-regulated dephosphorylation at the activating site of inhibitor-1 (Thr 35) followed by dissociation of the inhibitor-1-PP1 complex and then full PP1 activation to promote mitotic exit. Thus, Cdc2 both phosphorylates multiple mitotic substrates and inhibits their PP1-mediated dephosphorylation.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • 8-Bromo Cyclic Adenosine Monophosphate / pharmacology
  • Animals
  • CDC2 Protein Kinase
  • Cell Cycle / physiology
  • Cell Cycle Proteins / antagonists & inhibitors
  • Cell Cycle Proteins / metabolism*
  • Cyclic AMP-Dependent Protein Kinases / antagonists & inhibitors
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Cyclin B / metabolism
  • Cyclin B / pharmacology
  • Cyclin-Dependent Kinases
  • HeLa Cells
  • Humans
  • Mitosis / physiology*
  • Models, Biological
  • Okadaic Acid / pharmacology
  • Oocytes / drug effects
  • Oocytes / metabolism
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Binding / physiology
  • Protein Kinase Inhibitors / pharmacology
  • Protein Kinases / metabolism
  • Protein Phosphatase 1 / antagonists & inhibitors
  • Protein Phosphatase 1 / metabolism*
  • Protein Phosphatase 1 / pharmacology
  • Proteins / metabolism*
  • Proteins / pharmacology
  • Purines / pharmacology
  • Roscovitine
  • Threonine / metabolism
  • Xenopus Proteins / antagonists & inhibitors
  • Xenopus Proteins / metabolism
  • Xenopus laevis

Substances

  • Cell Cycle Proteins
  • Cyclin B
  • Phosphoproteins
  • Protein Kinase Inhibitors
  • Proteins
  • Purines
  • Xenopus Proteins
  • phosphoprotein phosphatase inhibitor 1
  • protein phosphatase inhibitor-2
  • Roscovitine
  • Okadaic Acid
  • 8-Bromo Cyclic Adenosine Monophosphate
  • Threonine
  • Protein Kinases
  • CDK1 protein, Xenopus
  • Cyclic AMP-Dependent Protein Kinases
  • CDC2 Protein Kinase
  • CDK1 protein, human
  • Cyclin-Dependent Kinases
  • Protein Phosphatase 1