Atg8-family interacting motif crucial for selective autophagy

被引:426
作者
Noda, Nobuo N. [1 ]
Ohsumi, Yoshinori [2 ]
Inagaki, Fuyuhiko [1 ]
机构
[1] Hokkaido Univ, Grad Sch Pharmaceut Sci, Dept Biol Struct, Kita Ku, Sapporo, Hokkaido 0600812, Japan
[2] Tokyo Inst Technol, Integrated Res Inst, Yokohama, Kanagawa 2268503, Japan
关键词
Selective autophagy; AIM; Cvt pathway; Mitophagy; p62; Atg8; VACUOLE TARGETING PATHWAY; RECEPTOR-ASSOCIATED PROTEIN; MAMMALIAN HOMOLOG; SORTING MECHANISM; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; CYTOPLASM; UBIQUITIN; LC3; DEGRADATION;
D O I
10.1016/j.febslet.2010.01.018
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
Autophagy is a bulk degradation system conserved among most eukaryotes. Recently, autophagy has been shown to mediate selective degradation of various targets such as aggregated proteins and damaged or superfluous organelles. Structural studies have uncovered the conserved specific interactions between autophagic receptors and Atg8-family proteins through WXXL-like sequences, which we term the Atg8-family interacting motif (AIM). AIM functions in various autophagic receptors such as Atg19 in the cytoplasm-to-vacuole targeting pathway, p62 and neighbor of BRCA1 gene 1 (NBR1) in autophagic degradation of protein aggregates, and Atg32 and Nix in mitophagy, and may link the target-receptor complex to autophagic membranes and/or their forming machineries. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:1379 / 1385
页数:7
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