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对逆转录复合物生理和病理作用的最新见解。

Updated Insight into the Physiological and Pathological Roles of the Retromer Complex.

作者信息

Abubakar Yakubu Saddeeq, Zheng Wenhui, Olsson Stefan, Zhou Jie

机构信息

State Key Laboratory of Ecological Pest Control for Fujian and Taiwan Crops, College of Life Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China.

College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou 350002, China.

出版信息

Int J Mol Sci. 2017 Jul 25;18(8):1601. doi: 10.3390/ijms18081601.

DOI:10.3390/ijms18081601
PMID:28757549
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5577995/
Abstract

Retromer complexes mediate protein trafficking from the endosomes to the -Golgi network (TGN) or through direct recycling to the plasma membrane. In yeast, they consist of a conserved trimer of the cargo selective complex (CSC), Vps26-Vps35-Vps29 and a dimer of sorting nexins (SNXs), Vps5-Vps17. In mammals, the CSC interacts with different kinds of SNX proteins in addition to the mammalian homologues of Vps5 and Vps17, which further diversifies retromer functions. The retromer complex plays important roles in many cellular processes including restriction of invading pathogens. In this review, we summarize some recent developments in our understanding of the physiological and pathological functions of the retromer complex.

摘要

逆转录复合物介导蛋白质从内体运输到反式高尔基体网络(TGN),或通过直接循环回到质膜。在酵母中,它们由货物选择性复合物(CSC)的保守三聚体Vps26-Vps35-Vps29和分选连接蛋白(SNXs)的二聚体Vps5-Vps17组成。在哺乳动物中,除了Vps5和Vps17的哺乳动物同源物外,CSC还与不同类型的SNX蛋白相互作用,这进一步使逆转录复合物的功能多样化。逆转录复合物在包括限制入侵病原体在内的许多细胞过程中发挥重要作用。在这篇综述中,我们总结了在理解逆转录复合物的生理和病理功能方面的一些最新进展。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b0c8/5577995/9247c7a23c2b/ijms-18-01601-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b0c8/5577995/c57e10af34ba/ijms-18-01601-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b0c8/5577995/9247c7a23c2b/ijms-18-01601-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b0c8/5577995/c57e10af34ba/ijms-18-01601-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b0c8/5577995/9247c7a23c2b/ijms-18-01601-g002.jpg

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