Ordered Organelle Degradation during Starvation-induced Autophagy
Ordered Organelle Degradation during Starvation-induced Autophagy
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DOI：
10.1074/mcp.m800184-mcp200
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发表时间：
2008-12-01
影响因子：
7
通讯作者：
Andersen, Jens S.
中科院分区：
文献类型：
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作者：
Kristensen, Anders Riis;Schandorff, Soren;Andersen, Jens S.
在饥饿时，细胞经历自噬，这是一种在整个细胞器和长寿命蛋白质的周转中重要的细胞降解途径。饥饿诱导的蛋白质降解被认为是一个非特异性的整体降解过程。我们通过定量质谱研究了氨基酸饥饿诱导的自噬过程中的全球蛋白质动态，并在36小时的饥饿过程中记录了近1500个蛋白质谱。聚类分析记录的蛋白质图谱显示，胞质蛋白质降解迅速，而蛋白质注释到各种复合物和细胞器降解后，在不同的时间段。对蛋白质降解途径的抑制将溶酶体/自噬体系统确定为主要降解途径。因此，饥饿通过自噬诱导降解，这似乎是选择性的，并以有序的方式降解蛋白质，而不是像迄今为止预期的那样完全任意。Molecular & Cellular Proteomics 7：2419-2428，2008.
Upon starvation cells undergo autophagy, a cellular degradation pathway important in the turnover of whole organelles and long lived proteins. Starvation-induced protein degradation has been regarded as an unspecific bulk degradation process. We studied global protein dynamics during amino acid starvation-induced autophagy by quantitative mass spectrometry and were able to record nearly 1500 protein profiles during 36 h of starvation. Cluster analysis of the recorded protein profiles revealed that cytosolic proteins were degraded rapidly, whereas proteins annotated to various complexes and organelles were degraded later at different time periods. Inhibition of protein degradation pathways identified the lysosomal/autophagosomal system as the main degradative route. Thus, starvation induces degradation via autophagy, which appears to be selective and to degrade proteins in an ordered fashion and not completely arbitrarily as anticipated so far. Molecular & Cellular Proteomics 7: 2419-2428, 2008.