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Updated: Jun 11, 2026

Measuring Diurnal Rhythms in Autophagic and Proteasomal Flux
Published on: September 17, 2019
Quantitative proteomics for the analysis of spatio-temporal protein dynamics during autophagy
Andrea C Zimmermann1, Mostafa Zarei, Sven Eiselein
1Freiburg Institute for Advanced Studies (FRIAS), School of Life Sciences-LIFENET, University of Freiburg, Freiburg, Germany.
Abstract:
Stress-induced autophagy leads to major cellular remodeling. During autophagy, a new organelle, the autophagosome, is formed that shuttles cellular material to lysosomes for degradation. Quantitative mass spectrometry-based proteomics is a powerful research strategy for the description of spatio-temporal protein dynamics during autophagy. This technique allows the identification of protein-protein interactions and of specific post-translational modifications. In addition, current methods enable the in-depth characterization of cellular as well as organellar composition changes and the global analysis of signaling networks. Thus, a plastic picture of the cell can be drawn. In this review we describe recent advances in MS-based proteomics approaches and their implications for autophagy-related research questions.
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