Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
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DOI：
10.1016/s0092-8674(01)00434-2
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发表时间：
2001-07-27
期刊：
影响因子：
64.5
通讯作者：
Emr, SD
中科院分区：
文献类型：
--
作者：
Katzmann, DJ;Babst, M;Emr, SD
多泡体（MVB）途径既负责溶酶体水解酶的生物合成递送，也负责在溶酶体中降解的许多活化的细胞表面受体的下调。我们证明泛素化可以作为MVB途径分类的信号。此外，我们还鉴定了一个350 kDa的复合物ESCRT-I（由Vps23、Vps28和Vps37组成），该复合物可识别泛素化的MVB货物，其功能对MVB囊泡的分类是必需的。该识别事件依赖于Vps23中保守的ubc样结构域。我们认为ESCRT-I代表了内体分选机制的一个保守成分，它在酵母和哺乳动物细胞中都起作用，将泛素修饰与MVB途径中的蛋白质分选和受体下调结合起来。
The multivesicular body (MVB) pathway is responsible for both the biosynthetic delivery of lysosomal hydrolases and the downregulation of numerous activated cell surface receptors which are degraded in the lysosome. We demonstrate that ubiquitination serves as a signal for sorting into the MVB pathway. In addition, we characterize a 350 kDa complex, ESCRT-I (composed of Vps23, Vps28, and Vps37), that recognizes ubiquitinated MVB cargo and whose function is required for sorting into MVB vesicles. This recognition event depends on a conserved UBC-like domain in Vps23. We propose that ESCRT-I represents a conserved component of the endosomal sorting machinery that functions in both yeast and mammalian cells to couple ubiquitin modification to protein sorting and receptor downregulation in the MVB pathway.