期刊
AUTOPHAGY
卷 12, 期 8, 页码 1411-1412出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/15548627.2016.1190891
关键词
basal autophagy; CCT; TRiC; degradative flux; proteasome; proteomics; ribosome; selective autophagy; turnover
类别
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R35GM119502] Funding Source: NIH RePORTER
- OFFICE OF THE DIRECTOR, NATIONAL INSTITUTES OF HEALTH [S10OD021486] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R35 GM119502] Funding Source: Medline
- NIH HHS [S10 OD021486] Funding Source: Medline
In eukaryotic cells, the macroautophagy pathway has been implicated in the degradation of long-lived proteins and damaged organelles. Although it has been demonstrated that macroautophagy can selectively degrade specific targets, its contribution to the basal turnover of cellular proteins had previously not been quantified on proteome-wide scales. In a recent study, we utilized dynamic proteomics to provide a global comparison of protein half-lives between wild-type and autophagy-deficient cells. Our results indicated that in quiescent fibroblasts, macroautophagy contributes to the basal turnover of a substantial fraction of the proteome. However, the contribution of macroautophagy to constitutive protein turnover is variable within the proteome. The methodology outlined in the study provides a global strategy for quantifying the selectivity of basal macroautophagy.
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