Autophagy proteins regulate ERK phosphorylation

• DOI: 10.1038/ncomms3799
• Publication Date: 2013-11-18T10:42:28Z
• Authors: Nuria Martinez-Lopez; Diana Athonvarangkul; Priti Mishall; Srabani Sahu; Rajat Singh
• Keywords: Male; Mitogen-Activated Protein Kinase Kinases; 0303 health sciences; Autophagy-Related Proteins; Down-Regulation; Autophagy-Related Protein 7; Article; Autophagy-Related Protein 5; Cell Line; Cysteine Endopeptidases; Mice; 03 medical and health sciences; Autophagy; Animals; Phosphorylation; Extracellular Signal-Regulated MAP Kinases; Microtubule-Associated Proteins

Abstract Autophagy is a conserved pathway that maintains cellular quality control. Extracellular signal-regulated kinase (ERK) controls various aspects of cell physiology including proliferation. Multiple signalling cascades, ERK, have been shown to regulate autophagy, however whether autophagy proteins (ATG) unknown. Here we show growth factor exposure increases the interaction ERK cascade components with ATG in cytosol and nucleus. its upstream MEK localize extra-luminal face autophagosomes. ERK2 interacts via substrate-binding domains. Deleting Atg7 or Atg5 blocking LC3 lipidation ATG5–ATG12 conjugation decreases phosphorylation. Conversely, increasing LC3-II availability by silencing cysteine protease ATG4B acute trehalose Decreased phosphorylation −/− cells does not occur from overactive phosphatases. Our findings thus reveal an unconventional function as scaffolds regulation