由GGA介导的甘露糖6-磷酸受体的分选

Sorting of mannose 6-phosphate receptors mediated by the GGAs.

作者信息

Puertollano R, Aguilar R C, Gorshkova I, Crouch R J, Bonifacino J S

机构信息

Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.

出版信息

Science. 2001 Jun 1;292(5522):1712-6. doi: 10.1126/science.1060750.

DOI:10.1126/science.1060750

PMID:11387475

Abstract

The delivery of soluble hydrolases to lysosomes is mediated by the cation-independent and cation-dependent mannose 6-phosphate receptors. The cytosolic tails of both receptors contain acidic-cluster-dileucine signals that direct sorting from the trans-Golgi network to the endosomal-lysosomal system. We found that these signals bind to the VHS domain of the Golgi-localized, gamma-ear-containing, ARF-binding proteins (GGAs). The receptors and the GGAs left the trans-Golgi network on the same tubulo-vesicular carriers. A dominant-negative GGA mutant blocked exit of the receptors from the trans-Golgi network. Thus, the GGAs appear to mediate sorting of the mannose 6-phosphate receptors at the trans-Golgi network.

摘要

可溶性水解酶向溶酶体的转运由不依赖阳离子和依赖阳离子的甘露糖6-磷酸受体介导。两种受体的胞质尾部均含有酸性簇双亮氨酸信号，该信号指导从反式高尔基体网络到内体-溶酶体系统的分选。我们发现这些信号与高尔基体定位的、含γ耳的、ARF结合蛋白（GGA）的VHS结构域结合。受体和GGA通过相同的管状小泡载体离开反式高尔基体网络。一种显性负性GGA突变体阻断了受体从反式高尔基体网络的输出。因此，GGA似乎在反式高尔基体网络中介导甘露糖6-磷酸受体的分选。