Chaperone-mediated autophagy: a unique way to enter the lysosome world

被引:639
作者
Kaushik, Susmita [1 ]
Cuervo, Ana Maria [1 ]
机构
[1] Albert Einstein Coll Med, Marion Bessin Liver Res Ctr, Inst Aging Studies, Dept Dev & Mol Biol, Bronx, NY 10461 USA
基金
美国国家卫生研究院;
关键词
aging; cancer; chaperones; lysosomes; membrane proteins; neurodegeneration; protein degradation; ALPHA-SYNUCLEIN; RAT-LIVER; SELECTIVE PATHWAY; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; CYTOSOLIC PROTEINS; PEPTIDE SEQUENCES; RIBONUCLEASE-A; DEGRADATION; PROTEASOME; RECEPTOR;
D O I
10.1016/j.tcb.2012.05.006
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
All cellular proteins undergo continuous synthesis and degradation. This permanent renewal is necessary to maintain a functional proteome and to allow rapid changes in levels of specific proteins with regulatory purposes. Although for a long time lysosomes were considered unable to contribute to the selective degradation of individual proteins, the discovery of chaperone-mediated autophagy (CMA) changed this notion. Here, we review the characteristics that set CMA apart from other types of lysosomal degradation and the subset of molecules that confer cells the capability to identify individual cytosolic proteins and direct them across the lysosomal membrane for degradation.
引用
收藏
页码:407 / 417
页数:11
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