Degradation of protein translation machinery by amino acid starvation-induced macroautophagy. Issue 6 (3rd June 2017)

• Record Type: Journal Article
• Authors: Gretzmeier, Christine; Eiselein, Sven; Johnson, Gregory R.; Engelke, Rudolf; Nowag, Heike; Zarei, Mostafa; Küttner, Victoria; Becker, Andrea C.; Rigbolt, Kristoffer T. G.; Høyer-Hansen, Maria; Andersen, Jens S.; Münz, Christian; Murphy, Robert F.; Dengjel, Jörn
• Is Part Of: Autophagy. Volume 13:Issue 6(2017)
• Page Start: 1064
• Page End: 1075
• Publication Date: 2017-06-03
• Subjects: autophagy -- degradation -- mass spectrometry -- protein turnover -- proteomics -- SILAC; Autophagic vacuoles -- Periodicals; Apoptosis -- Periodicals; Cell death -- Periodicals; Lysosomes -- Periodicals; Degeneration (Pathology) -- Periodicals; Autophagy -- Periodicals; Cell Death -- Periodicals; Lysosomes -- Periodicals; Periodicals; 571.936
• DOI: 10.1080/15548627.2016.1274485
• Languages: English
• ISSNs: 1554-8627

Abstract

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.