Interplay between Cdh1 and JNK activity during the cell cycle

Nat Cell Biol. 2010 Jul;12(7):686-95. doi: 10.1038/ncb2071. Epub 2010 Jun 27.

Abstract

The ubiquitin ligase APC/C(Cdh1) coordinates degradation of key cell cycle regulators. We report here that a nuclear-localized portion of the stress-activated kinase JNK is degraded by the APC/C(Cdh1) during exit from mitosis and the G1 phase of the cell cycle. Expression of a non-degradable JNK induces prometaphase-like arrest and aberrant mitotic spindle dynamics. Moreover, JNK phosphorylates Cdh1 directly, during G2 and early mitosis, changing its subcellular localization and attenuating its ability to activate the APC/C during G2/M. This regulatory mechanism between JNK and Cdh1 reveals an important function for JNK during the cell cycle.

Publication types

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

MeSH terms

  • Antigens, CD
  • Cadherins / metabolism*
  • Cell Cycle / physiology*
  • Cell Line
  • Flow Cytometry
  • G1 Phase / physiology
  • HeLa Cells
  • Humans
  • Immunoprecipitation
  • MAP Kinase Kinase 4 / metabolism*
  • Mitosis / physiology
  • Phosphorylation

Substances

  • Antigens, CD
  • CDH1 protein, human
  • Cadherins
  • MAP Kinase Kinase 4