Interactions between Autophagy Receptors and Ubiquitin-like Proteins Form the Molecular Basis for Selective Autophagy

被引:787
作者
Rogov, Vladimir [1 ,2 ]
Doetsch, Volker [1 ,2 ]
Johansen, Terje [3 ]
Kirkin, Vladimir [4 ]
机构
[1] Goethe Univ Frankfurt, Inst Biophys Chem, D-60439 Frankfurt, Germany
[2] Goethe Univ Frankfurt, Ctr Biomol Magnet Resonance, D-60439 Frankfurt, Germany
[3] Univ Tromso, Inst Med Biol, Mol Canc Res Grp, N-9037 Tromso, Norway
[4] Merck KGaA, D-64293 Darmstadt, Germany
关键词
TRANSCRIPTION FACTOR NRF2; ATG8-PE DECONJUGATION; TAGS PEROXISOMES; STRUCTURAL BASIS; DEGRADATION; P62; BIOGENESIS; MECHANISM; LC3; P62/SQSTM1;
D O I
10.1016/j.molcel.2013.12.014
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
Selective autophagy ensures recognition and removal of various cytosolic cargos. Hence, aggregated proteins, damaged organelles, or pathogens are enclosed into the double-membrane vesicle, the autophagosome, and delivered to the lysosome for degradation. This process is mediated by selective autophagy receptors, such as p62/SQSTM1. These proteins recognize autophagic cargo and, via binding to small ubiquitin-like modifiers (UBLs)-Atg8/LC3/GABARAPs and ATG5-mediate formation of selective autophagosomes. Recently, it was found that UBLs can directly engage the autophagosome nucleation machinery. Here, we review recent findings on selective autophagy and propose a model for selective autophagosome formation in close proximity to cargo.
引用
收藏
页码:167 / 178
页数:12
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