Ordered bulk degradation via autophagy
Ordered bulk degradation via autophagy
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DOI：
10.4161/auto.6824
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发表时间：
2008-11-16
期刊：
影响因子：
13.3
通讯作者：
Andersen, Jens S.
中科院分区：
文献类型：
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作者：
Dengiel, Joern;Kristensen, Anders Riis;Andersen, Jens S.
在氨基酸饥饿过程中，细胞发生大自噬，这被认为是一种非特异性的整体降解过程。最近，越来越多的细胞器特异性自噬亚型，如网状吞噬，线粒体自噬和核糖体自噬已被描述，它可以显示，根据实验设置，自噬特异性地可以删除某些亚细胞成分。我们使用了一种无偏的定量蛋白质组学方法，依赖于稳定同位素标记的氨基酸在细胞培养（SILAC），研究全球蛋白质动力学在氨基酸饥饿诱导的自噬。观察蛋白酶体和溶酶体降解，两种降解途径之间的充分串扰变得明显。通过自噬的降解似乎是有序的，并在蛋白质复合物/细胞器水平进行调节。这提出了几个重要的问题，例如：宏自噬本身是否具有特异性，以及它在饥饿期间的作用是什么？
During amino acid starvation cells undergo macroautophagy which is regarded as art unspecific bulk degradation process. Lately, more and more organelle-specific autophagy subtypes such as reticulophagy, mitophagy and ribophagy have been described and it could be shown, depending on the experimental setup, that autophagy specifically can remove certain subcellular components. We used an unbiased quantitative proteomics approach relying on stable isotope labeling by amino acids in cell culture (SILAC) to study global protein dynamics during amino acid starvation-induced autophagy. Looking at proteasomal and lysosomal degradation ample cross-talk between the two degradation pathways became evident. Degradation via autophagy appeared to be ordered and regulated at the protein complex/organelle level. This raises several important questions such as: can macroautophagy itself be specific and what is its role during starvation?