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Golgi structure formation, function, and post-translational modifications in mammalian cells

The Golgi apparatus is a central membrane organelle for trafficking and post-translational modifications of proteins and lipids in cells. In mammalian cells, it is organized in the form of stacks of tightly aligned flattened cisternae, and dozens of stacks are often linked laterally into a ribbon-li...

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Detalles Bibliográficos
Autores principales: Huang, Shijiao, Wang, Yanzhuang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: F1000 Research Limited 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5710388/
https://www.ncbi.nlm.nih.gov/pubmed/29225785
http://dx.doi.org/10.12688/f1000research.11900.1
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author Huang, Shijiao
Wang, Yanzhuang
author_facet Huang, Shijiao
Wang, Yanzhuang
author_sort Huang, Shijiao
collection PubMed
description The Golgi apparatus is a central membrane organelle for trafficking and post-translational modifications of proteins and lipids in cells. In mammalian cells, it is organized in the form of stacks of tightly aligned flattened cisternae, and dozens of stacks are often linked laterally into a ribbon-like structure located in the perinuclear region of the cell. Proper Golgi functionality requires an intact architecture, yet Golgi structure is dynamically regulated during the cell cycle and under disease conditions. In this review, we summarize our current understanding of the relationship between Golgi structure formation, function, and regulation, with focus on how post-translational modifications including phosphorylation and ubiquitination regulate Golgi structure and on how Golgi unstacking affects its functions, in particular, protein trafficking, glycosylation, and sorting in mammalian cells.
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spelling pubmed-57103882017-12-07 Golgi structure formation, function, and post-translational modifications in mammalian cells Huang, Shijiao Wang, Yanzhuang F1000Res Review The Golgi apparatus is a central membrane organelle for trafficking and post-translational modifications of proteins and lipids in cells. In mammalian cells, it is organized in the form of stacks of tightly aligned flattened cisternae, and dozens of stacks are often linked laterally into a ribbon-like structure located in the perinuclear region of the cell. Proper Golgi functionality requires an intact architecture, yet Golgi structure is dynamically regulated during the cell cycle and under disease conditions. In this review, we summarize our current understanding of the relationship between Golgi structure formation, function, and regulation, with focus on how post-translational modifications including phosphorylation and ubiquitination regulate Golgi structure and on how Golgi unstacking affects its functions, in particular, protein trafficking, glycosylation, and sorting in mammalian cells. F1000 Research Limited 2017-11-27 /pmc/articles/PMC5710388/ /pubmed/29225785 http://dx.doi.org/10.12688/f1000research.11900.1 Text en Copyright: © 2017 Huang S and Wang Y http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Huang, Shijiao
Wang, Yanzhuang
Golgi structure formation, function, and post-translational modifications in mammalian cells
title Golgi structure formation, function, and post-translational modifications in mammalian cells
title_full Golgi structure formation, function, and post-translational modifications in mammalian cells
title_fullStr Golgi structure formation, function, and post-translational modifications in mammalian cells
title_full_unstemmed Golgi structure formation, function, and post-translational modifications in mammalian cells
title_short Golgi structure formation, function, and post-translational modifications in mammalian cells
title_sort golgi structure formation, function, and post-translational modifications in mammalian cells
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5710388/
https://www.ncbi.nlm.nih.gov/pubmed/29225785
http://dx.doi.org/10.12688/f1000research.11900.1
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