Quantitative proteomics for the analysis of spatio-temporal protein dynamics during autophagy

被引:24
作者
Zimmermann, Andrea C. [1 ,2 ]
Zarei, Mostafa [1 ,2 ]
Eiselein, Sven [1 ,2 ,3 ]
Dengjel, Joern [1 ,2 ,3 ]
机构
[1] Univ Freiburg, Sch Life Sci LIFENET, Freiburg Inst Adv Studies FRIAS, Freiburg, Germany
[2] Univ Freiburg, Ctr Biol Syst Anal, Freiburg, Germany
[3] Univ Freiburg, Ctr Biol Signaling Studies BIOSS, Freiburg, Germany
关键词
mass spectrometry; quantitative proteomics; organellar proteomics; phosphoproteomics; signaling; autophagy; post-translational modification; MASS-SPECTROMETRY; SELECTIVE AUTOPHAGY; CELL-DEATH; PHOSPHORYLATION; DEGRADATION; MACROAUTOPHAGY; STARVATION; PHOSPHOPROTEOMICS; QUANTIFICATION; LOCALIZATION;
D O I
10.4161/auto.6.8.12786
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
引用
收藏
页码:1009 / 1016
页数:8
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