Assessment of Posttranslational Modifications of ATG proteins

被引：3
作者：
Xie, Y. [1 ,2 ]
Kang, R. [1 ]
Tang, D. [1 ]
机构：
[1] Univ Pittsburgh, Pittsburgh, PA 15260 USA
[2] Cent S Univ, Xiangya Hosp, Changsha, Hunan, Peoples R China
来源：
MOLECULAR CHARACTERIZATION OF AUTOPHAGIC RESPONSES, PT A | 2017年 / 587卷
关键词：
BECLIN; 1; AUTOPHAGY; PHOSPHORYLATION; MACROAUTOPHAGY; ULK1; AMPK; UBIQUITINATION; MACHINERY; COMPLEXES; LC3;
D O I：
10.1016/bs.mie.2016.09.057
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Posttranslational modifications (PTMs) increase the functional diversity of proteins and play a key role in many cellular processes. Macroautophagy (hereafter simply referred to as autophagy) is an evolutionarily conserved, lysosome-dependent degradation pathway. This process is finely regulated by autophagy-related (ATG) genes widely conserved among eukaryotes from yeast to mammals. Various PTMs of ATG proteins such as phosphorylation, ubiquitination, and acetylation have been theorized to play a critical role in modulating autophagic processes and activity. In this chapter, we introduce several antibody-based tools (e.g., Western blot, Simple Western T, immunofluorescence, and immunoprecipitation) that are widely used to assess the PTMs of ATG proteins in mammalian cells.
引用
收藏
页码：171 / 188
页数：18
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