Selective autophagy

被引:0
|
作者
Svenning, Steingrim [1 ]
Johansen, Terje [1 ]
机构
[1] Univ Tromso, Mol Canc Res Grp, Inst Med Biol, N-9037 Tromso, Norway
来源
关键词
aggrephagy; NBR1; NDP52; optineurin; p62; selective autophagy; TBK1; ubiquitin; xenophagy; INCLUSION-BODY FORMATION; TAGS PEROXISOMES; STRUCTURAL BASIS; LIR MOTIF; PROTEIN; DEGRADATION; RECEPTOR; P62; P62/SQSTM1; NBR1;
D O I
10.1042/BSE0550079
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
During the last decade it has become evident that autophagy is not simply a non-selective bulk degradation pathway for intracellular components. On the contrary, the discovery and characterization of autophagy receptors which target specific cargo for lysosomal degradation by interaction with ATG8 (autophagy-related protein 8)/LC3 (light-chain 3) has accelerated our understanding of selective autophagy. A number of autophagy receptors have been identified which specifically mediate the selective autophagosomal degradation of a variety of cargoes including protein aggregates, signalling complexes, midbody rings, mitochondria and bacterial pathogens. In the present chapter, we discuss these autophagy receptors, their binding to ATG8/LC3 proteins and how they act in ubiquitin-mediated selective autophagy of intracellular bacteria (xenophagy) and protein aggregates (aggrephagy).
引用
收藏
页码:79 / 92
页数:14
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