Phosphoinositide kinase signaling controls ER-PM cross-talk

Mol Biol Cell. 2016 Apr 1;27(7):1170-80. doi: 10.1091/mbc.E16-01-0002. Epub 2016 Feb 10.

Abstract

Membrane lipid dynamics must be precisely regulated for normal cellular function, and disruptions in lipid homeostasis are linked to the progression of several diseases. However, little is known about the sensory mechanisms for detecting membrane composition and how lipid metabolism is regulated in response to membrane stress. We find that phosphoinositide (PI) kinase signaling controls a conserved PDK-TORC2-Akt signaling cascade as part of a homeostasis network that allows the endoplasmic reticulum (ER) to modulate essential responses, including Ca(2+)-regulated lipid biogenesis, upon plasma membrane (PM) stress. Furthermore, loss of ER-PM junctions impairs this protective response, leading to PM integrity defects upon heat stress. Thus PI kinase-mediated ER-PM cross-talk comprises a regulatory system that ensures cellular integrity under membrane stress conditions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3-Phosphoinositide-Dependent Protein Kinases / metabolism*
  • Cell Membrane / metabolism*
  • Endoplasmic Reticulum / metabolism*
  • Lipid Metabolism*
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae / physiology
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Signal Transduction*
  • Stress, Physiological

Substances

  • Saccharomyces cerevisiae Proteins
  • 3-Phosphoinositide-Dependent Protein Kinases
  • PKH1 protein, S cerevisiae
  • PKH2 protein, S cerevisiae