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首页> 外文期刊>Molecular cell >A role for ubiquitin in selective autophagy.
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A role for ubiquitin in selective autophagy.

机译：泛素在选择性自噬中的作用。

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摘要

Ubiquitination is the hallmark of protein degradation by the 26S proteasome. However, the proteasome is limited in its capacity to degrade oligomeric and aggregated proteins. Removal of harmful protein aggregates is mediated by autophagy, a mechanism by which the cell sequesters cytosolic cargo and delivers it for degradation by the lysosome. Identification of autophagy receptors, such as p62/SQSTM1 and NBR1, which simultaneously bind both ubiquitin and autophagy-specific ubiquitin-like modifiers, LC3/GABARAP, has provided a molecular link between ubiquitination and autophagy. This review explores the hypothesis that ubiquitin represents a selective degradation signal suitable for targeting various types of cargo, ranging from protein aggregates to membrane-bound organelles and microbes.
机译：泛素化是26S蛋白酶降解蛋白质的标志。但是，蛋白酶体降解寡聚体和聚集蛋白的能力受到限制。有害蛋白质聚集体的去除是通过自噬介导的，自噬是细胞隔离胞质货物并通过溶酶体降解的机制。能够同时结合泛素和自噬特异性泛素样修饰剂LC3 / GABARAP的自噬受体（例如p62 / SQSTM1和NBR1）的鉴定提供了泛素化和自噬之间的分子联系。这篇综述探讨了泛素代表适合于针对各种类型货物的选择性降解信号的假设，从蛋白质聚集体到膜结合的细胞器和微生物。

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