Degradation of protein translation machinery by amino acid starvation-induced macroautophagy
Open Access
- 26 May 2017
- journal article
- research article
- Published by Taylor & Francis Ltd in Autophagy
- Vol. 13 (6), 1064-1075
- https://doi.org/10.1080/15548627.2016.1274485
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.This publication has 41 references indexed in Scilit:
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