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Folding and Quality Control of Glycoproteins
Folding of proteins is essential so that they can exert their functions. For proteins that transit the secretory pathway, folding occurs in the endoplasmic reticulum (ER) and various chaperone systems assist in acquiring their correct folding/subunit formation. N-glycosylation is one of the most con...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7258711/ http://dx.doi.org/10.1016/B978-0-12-409547-2.14947-9 |
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author | Suzuki, Tadashi Fujihira, Haruhiko |
author_facet | Suzuki, Tadashi Fujihira, Haruhiko |
author_sort | Suzuki, Tadashi |
collection | PubMed |
description | Folding of proteins is essential so that they can exert their functions. For proteins that transit the secretory pathway, folding occurs in the endoplasmic reticulum (ER) and various chaperone systems assist in acquiring their correct folding/subunit formation. N-glycosylation is one of the most conserved posttranslational modification for proteins, and in eukaryotes it occurs in the ER. Consequently, eukaryotic cells have developed various systems that utilize N-glycans to dictate and assist protein folding, or if they consistently fail to fold properly, to destroy proteins for quality control and the maintenance of homeostasis of proteins in the ER. |
format | Online Article Text |
id | pubmed-7258711 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
record_format | MEDLINE/PubMed |
spelling | pubmed-72587112020-05-29 Folding and Quality Control of Glycoproteins Suzuki, Tadashi Fujihira, Haruhiko Comprehensive Glycoscience Article Folding of proteins is essential so that they can exert their functions. For proteins that transit the secretory pathway, folding occurs in the endoplasmic reticulum (ER) and various chaperone systems assist in acquiring their correct folding/subunit formation. N-glycosylation is one of the most conserved posttranslational modification for proteins, and in eukaryotes it occurs in the ER. Consequently, eukaryotic cells have developed various systems that utilize N-glycans to dictate and assist protein folding, or if they consistently fail to fold properly, to destroy proteins for quality control and the maintenance of homeostasis of proteins in the ER. 2021 2021-06-24 /pmc/articles/PMC7258711/ http://dx.doi.org/10.1016/B978-0-12-409547-2.14947-9 Text en Copyright © 2021 Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Suzuki, Tadashi Fujihira, Haruhiko Folding and Quality Control of Glycoproteins |
title | Folding and Quality Control of Glycoproteins |
title_full | Folding and Quality Control of Glycoproteins |
title_fullStr | Folding and Quality Control of Glycoproteins |
title_full_unstemmed | Folding and Quality Control of Glycoproteins |
title_short | Folding and Quality Control of Glycoproteins |
title_sort | folding and quality control of glycoproteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7258711/ http://dx.doi.org/10.1016/B978-0-12-409547-2.14947-9 |
work_keys_str_mv | AT suzukitadashi foldingandqualitycontrolofglycoproteins AT fujihiraharuhiko foldingandqualitycontrolofglycoproteins |