Dissecting the role of His domain protein tyrosine phosphatase/PTPN23 and ESCRTs in sorting activated epidermal growth factor receptor to the multivesicular body.

Dissecting the role of His domain protein tyrosine phosphatase/PTPN23 and ESCRTs in sorting activated epidermal growth factor receptor to the multivesicular body.
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DOI:
10.1042/bst20170443
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发表时间:
2018-10-19
影响因子:
3.9
通讯作者:
Woodman P
Woodman P
中科院分区:
生物学3区
文献类型:
--
作者:
Tabernero L;Woodman P

文献摘要

相似文献

将活化的表皮生长因子受体(EGFR)分选到多泡体(MVB)内的管腔内囊泡(ILV)中是受体下调过程中的重要步骤。驱动EGFR分选的机制附着于内体的细胞质面,并产生出芽进入内体腔的囊泡,但不知何故逃脱了自身的封装。这种机制被称为ESCRT(运输所需的内体分选复合物)途径,一系列多蛋白质复合物和辅助因子首先在酵母中发现。在这里,我们回顾了酵母ESCRT途径,并描述了相应的组件在哺乳动物细胞中的EGFR排序。其中之一是His结构域蛋白酪氨酸磷酸酶(HD-PTP/PTPN 23),我们审查涉及HD-PTP和ESCRT的相互作用。最后,我们描述了一个工作模型,如何ESCRT途径可能会克服内在的地形问题的EGFR分选MVB腔。
Sorting of activated epidermal growth factor receptor (EGFR) into intraluminal vesicles (ILVs) within the multivesicular body (MVB) is an essential step during the down-regulation of the receptor. The machinery that drives EGFR sorting attaches to the cytoplasmic face of the endosome and generates vesicles that bud into the endosome lumen, but somehow escapes encapsulation itself. This machinery is termed the ESCRT (endosomal sorting complexes required for transport) pathway, a series of multi-protein complexes and accessory factors first identified in yeast. Here, we review the yeast ESCRT pathway and describe the corresponding components in mammalian cells that sort EGFR. One of these is His domain protein tyrosine phosphatase (HD-PTP/PTPN23), and we review the interactions involving HD-PTP and ESCRTs. Finally, we describe a working model for how this ESCRT pathway might overcome the intrinsic topographical problem of EGFR sorting to the MVB lumen.