Autophagy: links with the proteasome
Autophagy: links with the proteasome
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DOI：
10.1016/j.ceb.2009.11.002
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发表时间：
2010-04-01
影响因子：
7.5
通讯作者：
Johansen, Terje
中科院分区：
文献类型：
--
作者：
Lamark, Trond;Johansen, Terje
真核细胞的两个主要蛋白质降解系统，泛素-蛋白酶体系统和自噬，一直被认为是完全独立的系统。然而，最近的研究结果强烈表明，这两条降解途径之间存在串扰甚至合作。泛素-蛋白酶体系统对错误折叠蛋白的泛素化和降解已被研究了一段时间，但对错误折叠蛋白的自噬降解却知之甚少。我们将在这里讨论最近的发现，这些发现揭示了决定错误折叠的蛋白质何时以及如何被特定地选择用于自噬降解的细胞过程，从而有利于蛋白酶体的降解。
The two main protein degradation systems of eukaryotic cells, the ubiquitin-proteasome system and autophagy, have been thought of as quite separate systems. However, recent findings strongly suggest that there is crosstalk and even cooperation between these two degradation pathways. Ubiquitination and degradation of misfolded proteins by the ubiquitin-proteasome system have been investigated for some time, but much less is known about autophagic degradation of misfolded proteins. We will here discuss recent findings that shed some light on the cellular processes deciding when and how misfolded proteins are specifically selected for autophagic degradation in favor of proteasomal degradation.