The M phase kinase Greatwall (Gwl) promotes inactivation of PP2A/B55delta, a phosphatase directed against CDK phosphosites

Mol Biol Cell. 2009 Nov;20(22):4777-89. doi: 10.1091/mbc.e09-07-0643. Epub 2009 Sep 30.

Abstract

We have previously shown that Greatwall kinase (Gwl) is required for M phase entry and maintenance in Xenopus egg extracts. Here, we demonstrate that Gwl plays a crucial role in a novel biochemical pathway that inactivates, specifically during M phase, "antimitotic" phosphatases directed against phosphorylations catalyzed by cyclin-dependent kinases (CDKs). A major component of this phosphatase activity is heterotrimeric PP2A containing the B55delta regulatory subunit. Gwl is activated during M phase by Cdk1/cyclin B (MPF), but once activated, Gwl promotes PP2A/B55delta inhibition with no further requirement for MPF. In the absence of Gwl, PP2A/B55delta remains active even when MPF levels are high. The removal of PP2A/B55delta corrects the inability of Gwl-depleted extracts to enter M phase. These findings support the hypothesis that M phase requires not only high levels of MPF function, but also the suppression, through a Gwl-dependent mechanism, of phosphatase(s) that would otherwise remove MPF-driven phosphorylations.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcineurin / metabolism
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2 / metabolism
  • Cell Division / physiology*
  • Cyclin-Dependent Kinases / metabolism*
  • Enzyme Inhibitors / pharmacology
  • Maturation-Promoting Factor / genetics
  • Maturation-Promoting Factor / metabolism
  • Okadaic Acid / pharmacology
  • Oocytes / cytology
  • Oocytes / drug effects
  • Oocytes / metabolism
  • Phosphorylation
  • Protein Phosphatase 2 / antagonists & inhibitors
  • Protein Phosphatase 2 / genetics
  • Protein Phosphatase 2 / metabolism*
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*
  • Protein Subunits / genetics
  • Protein Subunits / metabolism
  • Xenopus Proteins / genetics
  • Xenopus Proteins / metabolism*
  • Xenopus laevis

Substances

  • Enzyme Inhibitors
  • Protein Subunits
  • Xenopus Proteins
  • Okadaic Acid
  • MASTL protein, Xenopus
  • Protein Serine-Threonine Kinases
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Cyclin-Dependent Kinases
  • Maturation-Promoting Factor
  • Calcineurin
  • Protein Phosphatase 2