AMPK connects energy stress to PIK3C3/VPS34 regulation

Autophagy. 2013 Jul;9(7):1110-1. doi: 10.4161/auto.24877. Epub 2013 May 2.

Abstract

The class III phosphatidylinositol (PtdIns)-3 kinase, PIK3C3/VPS34, forms multiple complexes and regulates a variety of cellular functions, especially in intracellular vesicle trafficking and autophagy. Even though PtdIns3P, the product of PIK3C3, is thought to be a critical membrane marker for the autophagosome, it is unclear how PIK3C3 is regulated in response to autophagy-inducing stimuli. A complexity of PIK3C3 biology is due in part to the existence of multiple complexes, of which the ATG14- or UVRAG-containing complexes play important roles in autophagy. We recently discovered differential regulation of distinct PIK3C3 complexes in response to energy starvation and showed a mechanism by which AMPK directly phosphorylates PIK3C3 and BECN1 to regulate non- and pro-autophagic PIK3C3 complexes, respectively.

Keywords: AMPK; ATG14; BECN1; VPS34 complexes; autophagy.

Publication types

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

MeSH terms

  • AMP-Activated Protein Kinases / metabolism*
  • Animals
  • Class III Phosphatidylinositol 3-Kinases / metabolism*
  • Embryo, Mammalian / cytology
  • Energy Metabolism*
  • Fibroblasts / metabolism
  • Humans
  • Mice
  • Models, Biological
  • Stress, Physiological*

Substances

  • Class III Phosphatidylinositol 3-Kinases
  • AMP-Activated Protein Kinases