Switching off IMMP2L signaling drives senescence via simultaneous metabolic alteration and blockage of cell death

Cell Res. 2018 Jun;28(6):625-643. doi: 10.1038/s41422-018-0043-5. Epub 2018 May 28.

Abstract

Cellular senescence is a fundamental cell fate playing a significant role throughout the natural aging process. However, the molecular determinants distinguishing senescence from other cell-cycle arrest states such as quiescence and post-mitotic state, and the specified mechanisms underlying cell-fate decisions towards senescence versus cell death in response to cellular stress stimuli remain less understood. Employing multi-omics approaches, we revealed that switching off the specific mitochondrial processing machinery involving the peptidase IMMP2L serves as the foundation of the senescence program, which was also observed during the mammalian aging process. Mechanistically, we demonstrate that IMMP2L processes and thus activates at least two substrates, mitochondrial metabolic enzyme glycerol-3-phosphate dehydrogenase (GPD2) and cell death regulator apoptosis-inducing factor (AIF). For cells destined to senesce, concerted shutdown of the IMMP2L-GPD2 and IMMP2L-AIF signaling axes collaboratively drives the senescent process by reprogramming mitochondria-associated redox status, phospholipid metabolism and signaling network, and simultaneously blocking cell death under oxidative stress conditions.

Publication types

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

MeSH terms

  • Aging
  • Animals
  • Apoptosis Inducing Factor / metabolism*
  • Cell Death
  • Cell Line
  • Cellular Senescence*
  • Endopeptidases / metabolism*
  • Glycerolphosphate Dehydrogenase / metabolism*
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Mice, Inbred C57BL
  • Oxidative Stress
  • Signal Transduction*

Substances

  • Apoptosis Inducing Factor
  • Glycerolphosphate Dehydrogenase
  • Endopeptidases
  • IMMP2L protein, human