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Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65
The Golgi receives the entire output of newly synthesized cargo from the endoplasmic reticulum (ER), processes it in the stack largely through modification of bound oligosaccharides, and sorts it in the trans-Golgi network (TGN). GRASP65 and GRASP55, two proteins localized to the Golgi stack and ear...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3620728/ https://www.ncbi.nlm.nih.gov/pubmed/23552074 http://dx.doi.org/10.1038/ncomms2669 |
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author | Xiang, Yi Zhang, Xiaoyan Nix, David B. Katoh, Toshihiko Aoki, Kazuhiro Tiemeyer, Michael Wang, Yanzhuang |
author_facet | Xiang, Yi Zhang, Xiaoyan Nix, David B. Katoh, Toshihiko Aoki, Kazuhiro Tiemeyer, Michael Wang, Yanzhuang |
author_sort | Xiang, Yi |
collection | PubMed |
description | The Golgi receives the entire output of newly synthesized cargo from the endoplasmic reticulum (ER), processes it in the stack largely through modification of bound oligosaccharides, and sorts it in the trans-Golgi network (TGN). GRASP65 and GRASP55, two proteins localized to the Golgi stack and early secretory pathway, mediate processes including Golgi stacking, Golgi ribbon linking, and unconventional secretion. Previously we have shown that GRASP depletion in cells disrupts Golgi stack formation. Here we report that knockdown of the GRASP proteins, alone or combined, accelerates protein trafficking through the Golgi membranes but also has striking negative effects on protein glycosylation and sorting. These effects are not caused by Golgi ribbon unlinking, unconventional secretion, or ER stress. We propose that GRASP55/65 are negative regulators of exocytic transport and that this slowdown helps to ensure more complete protein glycosylation in the Golgi stack and proper sorting at the TGN. |
format | Online Article Text |
id | pubmed-3620728 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
record_format | MEDLINE/PubMed |
spelling | pubmed-36207282013-10-03 Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65 Xiang, Yi Zhang, Xiaoyan Nix, David B. Katoh, Toshihiko Aoki, Kazuhiro Tiemeyer, Michael Wang, Yanzhuang Nat Commun Article The Golgi receives the entire output of newly synthesized cargo from the endoplasmic reticulum (ER), processes it in the stack largely through modification of bound oligosaccharides, and sorts it in the trans-Golgi network (TGN). GRASP65 and GRASP55, two proteins localized to the Golgi stack and early secretory pathway, mediate processes including Golgi stacking, Golgi ribbon linking, and unconventional secretion. Previously we have shown that GRASP depletion in cells disrupts Golgi stack formation. Here we report that knockdown of the GRASP proteins, alone or combined, accelerates protein trafficking through the Golgi membranes but also has striking negative effects on protein glycosylation and sorting. These effects are not caused by Golgi ribbon unlinking, unconventional secretion, or ER stress. We propose that GRASP55/65 are negative regulators of exocytic transport and that this slowdown helps to ensure more complete protein glycosylation in the Golgi stack and proper sorting at the TGN. 2013 /pmc/articles/PMC3620728/ /pubmed/23552074 http://dx.doi.org/10.1038/ncomms2669 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Xiang, Yi Zhang, Xiaoyan Nix, David B. Katoh, Toshihiko Aoki, Kazuhiro Tiemeyer, Michael Wang, Yanzhuang Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65 |
title | Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65 |
title_full | Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65 |
title_fullStr | Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65 |
title_full_unstemmed | Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65 |
title_short | Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65 |
title_sort | regulation of protein glycosylation and sorting by the golgi matrix proteins grasp55/65 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3620728/ https://www.ncbi.nlm.nih.gov/pubmed/23552074 http://dx.doi.org/10.1038/ncomms2669 |
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