Endosomal transport via ubiquitination.
Endosomal transport via ubiquitination.
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DOI：
10.1016/j.tcb.2011.08.007
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发表时间：
2011-11
影响因子：
19
通讯作者：
Lehner PJ
中科院分区：
文献类型：
--
作者：
Piper RC;Lehner PJ
细胞的存活、生长、分化和稳态都依赖于对特定细胞表面膜蛋白丰度的精确控制。细胞表面蛋白质必须对环境和细胞内信号做出适当的反应，通常经历调节的内化和溶酶体降解。此外，细胞表面蛋白质可以承受损伤，必须被识别和去除。现在已经出现了一种统一的机制，用于将受损和下调的蛋白质通过与泛素的连接运输到溶酶体，泛素作为网格蛋白介导的内化和分选到晚期内体内腔的分选信号。主要的问题仍然是这个广泛的系统是如何管理的，它是如何适应，以满足特定的细胞表面蛋白的需要，以及是否Ub作为一个以上的单程票溶酶体降解。在这里，我们强调最近对这些问题的见解和仍然存在的挑战。
Cell survival, growth, differentiation, and homeostasis all rely on exquisite control over the abundance of particular cell surface membrane proteins. Cell surface proteins must respond appropriately to environmental as well as intracellular cues, often undergoing regulated internalization and lysosomal degradation. In addition, cell surface proteins can sustain damage and must be recognized and removed. A unifying mechanism has now emerged for the trafficking of damaged and downregulated proteins to the lysosome by their attachment to ubiquitin, which serves as a sorting signal for clathrin-mediated internalization and sorting into the lumen of late endosomes. Major questions remain as to how this broad system is governed, how it is adapted to meet the needs of particular cell surface proteins, and whether Ub serves as more than a one-way ticket to the lysosome for degradation. Here we highlight recent insights into these questions and the challenges that remain.
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