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Updated Insight into the Physiological and Pathological Roles of the Retromer Complex
Retromer complexes mediate protein trafficking from the endosomes to the trans-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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5577995/ https://www.ncbi.nlm.nih.gov/pubmed/28757549 http://dx.doi.org/10.3390/ijms18081601 |
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author | Abubakar, Yakubu Saddeeq Zheng, Wenhui Olsson, Stefan Zhou, Jie |
author_facet | Abubakar, Yakubu Saddeeq Zheng, Wenhui Olsson, Stefan Zhou, Jie |
author_sort | Abubakar, Yakubu Saddeeq |
collection | PubMed |
description | Retromer complexes mediate protein trafficking from the endosomes to the trans-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. |
format | Online Article Text |
id | pubmed-5577995 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-55779952017-09-05 Updated Insight into the Physiological and Pathological Roles of the Retromer Complex Abubakar, Yakubu Saddeeq Zheng, Wenhui Olsson, Stefan Zhou, Jie Int J Mol Sci Review Retromer complexes mediate protein trafficking from the endosomes to the trans-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. MDPI 2017-07-25 /pmc/articles/PMC5577995/ /pubmed/28757549 http://dx.doi.org/10.3390/ijms18081601 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Abubakar, Yakubu Saddeeq Zheng, Wenhui Olsson, Stefan Zhou, Jie Updated Insight into the Physiological and Pathological Roles of the Retromer Complex |
title | Updated Insight into the Physiological and Pathological Roles of the Retromer Complex |
title_full | Updated Insight into the Physiological and Pathological Roles of the Retromer Complex |
title_fullStr | Updated Insight into the Physiological and Pathological Roles of the Retromer Complex |
title_full_unstemmed | Updated Insight into the Physiological and Pathological Roles of the Retromer Complex |
title_short | Updated Insight into the Physiological and Pathological Roles of the Retromer Complex |
title_sort | updated insight into the physiological and pathological roles of the retromer complex |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5577995/ https://www.ncbi.nlm.nih.gov/pubmed/28757549 http://dx.doi.org/10.3390/ijms18081601 |
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