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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).
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页码:79 / 92
页数:14
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