Ubiquitin-dependent sorting of integral membrane proteins for degradation in lysosomes
Ubiquitin-dependent sorting of integral membrane proteins for degradation in lysosomes
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DOI：
10.1016/j.ceb.2007.07.002
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发表时间：
2007-08-01
影响因子：
7.5
通讯作者：
Luzio, J. Paul
中科院分区：
文献类型：
--
作者：
Piper, Robert C.;Luzio, J. Paul
与我们对整合膜蛋白如何被分选并递送至溶酶体进行降解的知识相比，递送新合成的驻留在溶酶体中的蛋白的途径被充分理解。许多膜蛋白在泛素化后被分选到溶酶体，这提供了分选信号，其可以在TGN（trans-Golgi网络）、质膜或内体处进行分选以递送到内腔囊泡中。已经确定了可以潜在地移动泛素化整合膜货物蛋白的候选多组分机器，但是仍然需要大量的工作来确定这些候选机器中的哪些直接识别泛素化货物以及它们在识别后对货物做什么。在分选到内体的内腔囊泡中所需的机器的情况下，还确定了其他功能，包括分选和内体沿着微管移动之间的联系。
The pathways that deliver newly synthesized proteins that reside in lysosomes are well understood on comparison with our knowledge of how integral membrane proteins are sorted and delivered to the lysosome for degradation. Many membrane proteins are sorted to lysosomes following ubiquitination, which provides a sorting signal that can operate for sorting at the TGN (trans-Golgi network), at the plasma membrane or at the endosome for delivery into lumenal vesicles. Candidate multicomponent machines that can potentially move ubiquitinated integral membrane cargo proteins have been identified, but much work is still required to ascertain which of these candidates directly recognize ubiquitinated cargo and what they do with cargo after recognition. In the case of the machinery required for sorting into the lumenal vesicles of endosomes, other functions have also been determined including a link between sorting and movement of endosomes along microtubules.