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Acetylation in the regulation of autophagy
被引:154
|作者:
Xu, Yinfeng
[1
]
Wan, Wei
[2
,3
]
机构:
[1] Hunan First Normal Univ, Lab Basic Biol, Changsha, Hunan, Peoples R China
[2] Zhejiang Univ, Dept Biochem, Sch Med, Hangzhou, Zhejiang, Peoples R China
[3] Zhejiang Univ, Dept Thorac Surg, Sir Run Run Shaw Hosp, Sch Med, Hangzhou, Zhejiang, Peoples R China
来源:
基金:
中国国家自然科学基金;
关键词:
Acetylation;
acetyltransferase;
autophagy;
deacetylase;
post-translational modification;
PHOSPHATIDYLINOSITOL 3-KINASE COMPLEXES;
ACTIVATED PROTEIN-KINASE;
LYSOSOMAL BIOGENESIS;
SELECTIVE AUTOPHAGY;
PARKINSONS-DISEASE;
MEDIATED AUTOPHAGY;
DEACETYLASE SIRT1;
BECLIN;
P300;
DEGRADATION;
D O I:
10.1080/15548627.2022.2062112
中图分类号:
Q2 [细胞生物学];
学科分类号:
071009 ;
090102 ;
摘要:
Post-translational modifications, such as phosphorylation, ubiquitination and acetylation, play crucial roles in the regulation of autophagy. Acetylation has emerged as an important regulatory mechanism for autophagy. Acetylation regulates autophagy initiation and autophagosome formation by targeting core components of the ULK1 complex, the BECN1-PIK3C3 complex, and the LC3 lipidation system. Recent studies have shown that acetylation occurs on the key proteins participating in autophagic cargo assembly and autophagosome-lysosome fusion, such as SQSTM1/p62 and STX17. In addition, acetylation controls autophagy at the transcriptional level by targeting histones and the transcription factor TFEB. Here, we review the current knowledge on acetylation of autophagy proteins and their regulations and functions in the autophagy pathway with focus on recent findings.
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页码:379 / 387
页数:9
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