Degradation of protein translation machinery by amino acid starvation-induced macroautophagy

Christine Gretzmeier, Sven Eiselein, Gregory R. Johnson, Rudolf Engelke, Heike Nowag, Mostafa Zarei, Victoria Küttner, Andrea C. Becker, Kristoffer T.G. Rigbolt, Maria Høyer-Hansen, Jens S. Andersen, Christian Münz, Robert F. Murphy, Jörn Dengjel

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13 Citations (Scopus)

Abstract

Macroautophagy is regarded as a nonspecific bulk degradation process of cytoplasmic material within the lysosome. However, the process has mainly been studied by nonspecific bulk degradation assays using radiolabeling. In the present study we monitor protein turnover and degradation by global, unbiased approaches relying on quantitative mass spectrometry-based proteomics. Macroautophagy is induced by rapamycin treatment, and by amino acid and glucose starvation in differentially, metabolically labeled cells. Protein dynamics are linked to image-based models of autophagosome turnover. Depending on the inducing stimulus, protein as well as organelle turnover differ. Amino acid starvation-induced macroautophagy leads to selective degradation of proteins important for protein translation. Thus, protein dynamics reflect cellular conditions in the respective treatment indicating stimulus-specific pathways in stress-induced macroautophagy.

Original languageEnglish
Pages (from-to)1064-1075
Number of pages12
JournalAutophagy
Volume13
Issue number6
DOIs
Publication statusPublished - 3 Jun 2017
Externally publishedYes

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Keywords

  • autophagy
  • degradation
  • mass spectrometry
  • protein turnover
  • proteomics
  • SILAC

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Gretzmeier, C., Eiselein, S., Johnson, G. R., Engelke, R., Nowag, H., Zarei, M., Küttner, V., Becker, A. C., Rigbolt, K. T. G., Høyer-Hansen, M., Andersen, J. S., Münz, C., Murphy, R. F., & Dengjel, J. (2017). Degradation of protein translation machinery by amino acid starvation-induced macroautophagy. Autophagy, 13(6), 1064-1075. https://doi.org/10.1080/15548627.2016.1274485