Ubiquitin-Dependent Sorting in Endocytosis
Ubiquitin-Dependent Sorting in Endocytosis
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DOI：
10.1101/cshperspect.a016808
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发表时间：
2014-01-01
影响因子：
7.2
通讯作者：
Lukacs, Gergely L.
中科院分区：
文献类型：
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作者：
Piper, Robert C.;Dikic, Ivan;Lukacs, Gergely L.
当泛素(Ub)附着在质膜上的膜蛋白上时，它会引导它们通过一系列分选步骤，最终将它们运送到溶酶体的管腔，在那里它们经历完全的蛋白质分解。泛素是由一系列复合体识别的，这些复合体在许多囊泡运输步骤中起作用。泛素是质膜内化的分选信号，也是整合到多囊泡晚期内体的腔内小泡的主要信号。催化这些步骤的分选机器可以通过各种Ub结合结构域与Ub结合。同时，许多这些复合体本身是泛素化的，因此提供了过多的潜在机制来调节它们的活性。在这里，我们提供了一个概述如何选择膜蛋白的泛素化和去泛素化的内吞途径，以及如何解释泛素信号的内吞分选机制。
When ubiquitin (Ub) is attached to membrane proteins on the plasma membrane, it directs them through a series of sorting steps that culminate in their delivery to the lumen of the lysosome where they undergo complete proteolysis. Ubiquitin is recognized by a series of complexes that operate at a number of vesicle transport steps. Ubiquitin serves as a sorting signal for internalization at the plasma membrane and is the major signal for incorporation into intraluminal vesicles of multivesicular late endosomes. The sorting machineries that catalyze these steps can bind Ub via a variety of Ub-binding domains. At the same time, many of these complexes are themselves ubiquitinated, thus providing a plethora of potential mechanisms to regulate their activity. Here we provide an overview of how membrane proteins are selected for ubiquitination and deubiquitination within the endocytic pathway and how that ubiquitin signal is interpreted by endocytic sorting machineries.