Regulated degradation of Chk1 by chaperone-mediated autophagy in response to DNA damage

被引:171
作者
Park, Caroline [1 ,2 ,3 ]
Suh, Yousin [2 ,3 ]
Cuervo, Ana Maria [1 ,3 ]
机构
[1] Albert Einstein Coll Med, Dept Dev & Mol Biol, Bronx, NY 10461 USA
[2] Albert Einstein Coll Med, Dept Genet, Bronx, NY 10461 USA
[3] Albert Einstein Coll Med, Inst Aging Res, Bronx, NY 10461 USA
基金
美国国家卫生研究院;
关键词
LYSOSOMAL PROTEOLYSIS; OXIDATIVE STRESS; CHECKPOINT; PROTEINS; KINASE; ACTIVATION; BLOCKAGE; PATHWAY; ENZYME; ATR;
D O I
10.1038/ncomms7823
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Chaperone-mediated autophagy (CMA) is activated in response to cellular stressors to prevent cellular proteotoxicity through selective degradation of altered proteins in lysosomes. Reduced CMA activity contributes to the decrease in proteome quality in disease and ageing. Here, we report that CMA is also upregulated in response to genotoxic insults and that declined CMA functionality leads to reduced cell survival and genomic instability. This role of CMA in genome quality control is exerted through regulated degradation of activated checkpoint kinase 1 (Chk1) by this pathway after the genotoxic insult. Nuclear accumulation of Chk1 in CMA-deficient cells compromises cell cycle progression and prolongs the time that DNA damage persists in these cells. Furthermore, blockage of CMA leads to hyperphosphorylation and destabilization of the MRN (Mre11-Rad50-Nbs1) complex, which participates in early steps of particular DNA repair pathways. We propose that CMA contributes to maintain genome stability by assuring nuclear proteostasis.
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页数:14
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