Preparing a cell for nuclear envelope breakdown: Spatio-temporal control of phosphorylation during mitotic entry

Bioessays. 2014 Aug;36(8):757-65. doi: 10.1002/bies.201400040. Epub 2014 May 30.

Abstract

Chromosome segregation requires the ordered separation of the newly replicated chromosomes between the two daughter cells. In most cells, this requires nuclear envelope (NE) disassembly during mitotic entry and its reformation at mitotic exit. Nuclear envelope breakdown (NEB) results in the mixture of two cellular compartments. This process is controlled through phosphorylation of multiple targets by cyclin-dependent kinase 1 (Cdk1)-cyclin B complexes as well as other mitotic enzymes. Experimental evidence also suggests that nucleo-cytoplasmic transport of critical cell cycle regulators such as Cdk1-cyclin B complexes or Greatwall, a kinase responsible for the inactivation of PP2A phosphatases, plays a major role in maintaining the boost of mitotic phosphorylation thus preventing the potential mitotic collapse derived from NEB. These data suggest the relevance of nucleo-cytoplasmic transport not only to communicate cytoplasmic and nuclear compartments during interphase, but also to prepare cells for the mixture of these two compartments during mitosis.

Keywords: Cdk; Greatwall; Mastl; PP2A phosphatase; cell division cycle; cyclin; mitosis; phosphorylation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chromosome Segregation
  • Humans
  • Microtubule-Associated Proteins / physiology
  • Mitosis*
  • Nuclear Envelope / metabolism*
  • Phosphoric Monoester Hydrolases / physiology
  • Phosphorylation
  • Protein Processing, Post-Translational
  • Protein Transport
  • Protein-Serine-Threonine Kinases / physiology

Substances

  • Microtubule-Associated Proteins
  • MASTL protein, human
  • Protein-Serine-Threonine Kinases
  • Phosphoric Monoester Hydrolases