RETRIEVAL OF TGN PROTEINS FROM THE CELL-SURFACE REQUIRES ENDOSOMAL ACIDIFICATION
RETRIEVAL OF TGN PROTEINS FROM THE CELL-SURFACE REQUIRES ENDOSOMAL ACIDIFICATION
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DOI：
10.1002/j.1460-2075.1994.tb06514.x
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发表时间：
1994-05-15
期刊：
影响因子：
11.4
通讯作者：
MUNRO, S
中科院分区：
文献类型：
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作者：
CHAPMAN, RE;MUNRO, S
TGN 38是一种功能未知的蛋白质，位于哺乳动物细胞的trans-Golgi网络（TGN）中。它的细胞内分布是通过它被不断地从质膜回收来维持的。在本文中，我们表明，当细胞被处理，vith代理，如氯喹，中和酸性细胞器，运动的TGN 38沿着内吞途径被阻断。用第二种TGN蛋白（蛋白酶弗林蛋白酶）观察到相同的效果。我们发现，弗林蛋白酶的胞质尾区足以赋予氯喹敏感的TGN定位在异源蛋白上。这些结果意味着，内体的内部pH值的影响分选过程介导的信号在细胞质部分的蛋白质，并有意义的作用，内体功能的酸化。
TGN38 is a protein of unknown function located in the trans-Golgi network (TGN) of mammalian cells. Its intracellular distribution is maintained by it being continuously retrieved from the plasma membrane. In this paper we show that when cells are treated,vith agents such as chloroquine which neutralize acidic organelles, the movement of TGN38 along the endocytic pathway is blocked. The same effect is observed with a second TGN protein, the protease furin. We show that the cytoplasmic tail of furin is sufficient to confer a chloroquine-sensitive TGN localization on a heterologous protein. These results imply that the internal pH of endosomes affects sorting processes mediated by signals in the cytoplasmic portion of proteins and have implications for the role of acidification in endosomal function.