Autophagy-independent incorporation of GFP-LC3 into protein aggregates is dependent on its interaction with p62/SQSTM1

被引：44

作者：

Shvets, Elena ^{[1
]}

Elazar, Zvulun ^{[1
]}

机构：

[1] Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel

来源：

AUTOPHAGY | 2008年 / 4卷 / 08期

基金：

以色列科学基金会;

关键词：

LC3; p62/sequestosomel; autophagy; lysosome; protein aggregates;

D O I：

10.4161/auto.6823

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

LC3 is a widely used marker of autophagosomes in mammalian cells. However, in addition to its autophagosomal localization, GFP-LC3 is often found associated with protein aggregates that are formed in an autophagy-independent manner.(1) In addition, LC3 directly interacts with p62/SQSTM1 (hereafter named p62), a common constituent of protein aggregates. In our recent report, we mapped the regions in LC3 involved in its binding to p62 and showed that this binding is essential for the incorporation of p62 into autophagosomes. 2 Here we demonstrate that the autophagy-unrelated association of GFP-LC3 with protein aggregates is dependent on its interaction with p62.

引用

页码：1054 / 1056

页数：3

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