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Autophagy proteins regulate ERK phosphorylation.

Nuria Martinez-Lopez1, Diana Athonvarangkul, Priti Mishall

  • 11] Department of Medicine, Albert Einstein College of Medicine, Bronx, New York 10461, USA [2] Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.

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Autophagy proteins (ATG) unexpectedly regulate cell signaling by acting as scaffolds. These ATG proteins influence extracellular signal-regulated kinase (ERK) phosphorylation, revealing a novel role in cellular communication.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Signal Transduction

Background:

  • Autophagy is a fundamental cellular process for maintaining quality control.
  • Extracellular signal-regulated kinase (ERK) signaling pathways regulate critical cellular functions like proliferation.
  • The interplay between ERK signaling and autophagy is established, but the role of autophagy proteins in regulating cell signaling remains unclear.

Purpose of the Study:

  • To investigate whether autophagy proteins (ATG) regulate cell signaling pathways, specifically ERK phosphorylation.
  • To elucidate the mechanism by which ATG proteins might influence ERK signaling.

Main Methods:

  • Utilized techniques to observe the interaction of ERK cascade components with ATG proteins.
  • Investigated the localization of ERK and MEK in relation to autophagosomes.
  • Employed genetic modifications (deletions of Atg7, Atg5) and pharmacological interventions (LC3 lipidation, ATG4B silencing, trehalose exposure) to assess effects on ERK phosphorylation.

Main Results:

  • Growth factor stimulation enhanced the interaction between ERK cascade components and ATG proteins in both the cytosol and nucleus.
  • ERK and MEK were found to localize to the autophagosome.
  • Disruption of autophagy (e.g., Atg7 or Atg5 deletion, blocked LC3 lipidation) led to decreased ERK phosphorylation.
  • Enhancing LC3-II levels (via ATG4B silencing or trehalose) increased ERK phosphorylation.
  • The observed decrease in ERK phosphorylation in Atg5-deficient cells was not attributable to overactive phosphatases.

Conclusions:

  • Autophagy proteins (ATG) function unconventionally as cellular scaffolds.
  • These ATG proteins play a novel role in regulating the phosphorylation of the ERK signaling pathway.
  • This discovery provides new insights into the cross-talk between autophagy and signal transduction pathways.