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

来源：

AUTOPHAGY | 2010年 / 6卷 / 08期

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

页码：1009 / 1016

页数：8

共 104 条

[51] Selective degradation of mitochondria by mitophagy [J].