AMP-activated protein kinase induces a p53-dependent metabolic checkpoint

Mol Cell. 2005 Apr 29;18(3):283-93. doi: 10.1016/j.molcel.2005.03.027.

Abstract

Replicative cell division is an energetically demanding process that can be executed only if cells have sufficient metabolic resources to support a doubling of cell mass. Here we show that proliferating mammalian cells have a cell-cycle checkpoint that responds to glucose availability. The glucose-dependent checkpoint occurs at the G(1)/S boundary and is regulated by AMP-activated protein kinase (AMPK). This cell-cycle arrest occurs despite continued amino acid availability and active mTOR. AMPK activation induces phosphorylation of p53 on serine 15, and this phosphorylation is required to initiate AMPK-dependent cell-cycle arrest. AMPK-induced p53 activation promotes cellular survival in response to glucose deprivation, and cells that have undergone a p53-dependent metabolic arrest can rapidly reenter the cell cycle upon glucose restoration. However, persistent activation of AMPK leads to accelerated p53-dependent cellular senescence. Thus, AMPK is a cell-intrinsic regulator of the cell cycle that coordinates cellular proliferation with carbon source availability.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • AMP-Activated Protein Kinases
  • Animals
  • Cell Cycle / physiology*
  • Cell Line
  • Cell Proliferation
  • Cell Survival
  • Cellular Senescence
  • Fibroblasts / cytology
  • Fibroblasts / metabolism
  • Glucose / metabolism*
  • Humans
  • Mice
  • Multienzyme Complexes / metabolism*
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism*
  • Serine / metabolism
  • Tumor Suppressor Protein p53 / genetics
  • Tumor Suppressor Protein p53 / metabolism*

Substances

  • Multienzyme Complexes
  • Tumor Suppressor Protein p53
  • Serine
  • Protein Serine-Threonine Kinases
  • AMP-Activated Protein Kinases
  • Glucose