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Glycan Structures Contain Information for the Spatial Arrangement of Glycoproteins in the Plasma Membrane

Glycoconjugates at the cell surface are crucial for cells to communicate with each other and the extracellular microenvironment. While it is generally accepted that glycans are vectorial biopolymers, their information content is unclear. This report provides evidence that distinct N-glycan structure...

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Autores principales: Hall, M. Kristen, Weidner, Douglas A., Chen, Jian ming, Bernetski, Christopher J., Schwalbe, Ruth A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3765438/
https://www.ncbi.nlm.nih.gov/pubmed/24040379
http://dx.doi.org/10.1371/journal.pone.0075013
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author Hall, M. Kristen
Weidner, Douglas A.
Chen, Jian ming
Bernetski, Christopher J.
Schwalbe, Ruth A.
author_facet Hall, M. Kristen
Weidner, Douglas A.
Chen, Jian ming
Bernetski, Christopher J.
Schwalbe, Ruth A.
author_sort Hall, M. Kristen
collection PubMed
description Glycoconjugates at the cell surface are crucial for cells to communicate with each other and the extracellular microenvironment. While it is generally accepted that glycans are vectorial biopolymers, their information content is unclear. This report provides evidence that distinct N-glycan structures influence the spatial arrangement of two integral membrane glycoproteins, Kv3.1 and E-cadherin, at the adherent membrane which in turn alter cellular properties. Distinct N-glycan structures were generated by heterologous expression of these glycoproteins in parental and glycosylation mutant Chinese hamster ovary cell lines. Unlike the N-linked glycans, the O-linked glycans of the mutant cell lines are similar to those of the parental cell line. Western and lectin blots of total membranes and GFP immunopurified samples, combined with glycosidase digestion reactions, were employed to verify the glycoproteins had predominantly complex, oligomannose, and bisecting type N-glycans from Pro(-)5, Lec1, and Lec10B cell lines, respectively. Based on total internal reflection fluorescence and differential interference contrast microscopy techniques, and cellular assays of live parental and glycosylation mutant CHO cells, we propose that glycoproteins with complex, oligomannose or bisecting type N-glycans relay information for localization of glycoproteins to various regions of the plasma membrane in both a glycan-specific and protein-specific manner, and furthermore cell-cell interactions are required for deciphering much of this information. These distinct spatial arrangements also impact cell adhesion and migration. Our findings provide direct evidence that N-glycan structures of glycoproteins contribute significantly to the information content of cells.
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spelling pubmed-37654382013-09-13 Glycan Structures Contain Information for the Spatial Arrangement of Glycoproteins in the Plasma Membrane Hall, M. Kristen Weidner, Douglas A. Chen, Jian ming Bernetski, Christopher J. Schwalbe, Ruth A. PLoS One Research Article Glycoconjugates at the cell surface are crucial for cells to communicate with each other and the extracellular microenvironment. While it is generally accepted that glycans are vectorial biopolymers, their information content is unclear. This report provides evidence that distinct N-glycan structures influence the spatial arrangement of two integral membrane glycoproteins, Kv3.1 and E-cadherin, at the adherent membrane which in turn alter cellular properties. Distinct N-glycan structures were generated by heterologous expression of these glycoproteins in parental and glycosylation mutant Chinese hamster ovary cell lines. Unlike the N-linked glycans, the O-linked glycans of the mutant cell lines are similar to those of the parental cell line. Western and lectin blots of total membranes and GFP immunopurified samples, combined with glycosidase digestion reactions, were employed to verify the glycoproteins had predominantly complex, oligomannose, and bisecting type N-glycans from Pro(-)5, Lec1, and Lec10B cell lines, respectively. Based on total internal reflection fluorescence and differential interference contrast microscopy techniques, and cellular assays of live parental and glycosylation mutant CHO cells, we propose that glycoproteins with complex, oligomannose or bisecting type N-glycans relay information for localization of glycoproteins to various regions of the plasma membrane in both a glycan-specific and protein-specific manner, and furthermore cell-cell interactions are required for deciphering much of this information. These distinct spatial arrangements also impact cell adhesion and migration. Our findings provide direct evidence that N-glycan structures of glycoproteins contribute significantly to the information content of cells. Public Library of Science 2013-09-06 /pmc/articles/PMC3765438/ /pubmed/24040379 http://dx.doi.org/10.1371/journal.pone.0075013 Text en © 2013 Hall et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Hall, M. Kristen
Weidner, Douglas A.
Chen, Jian ming
Bernetski, Christopher J.
Schwalbe, Ruth A.
Glycan Structures Contain Information for the Spatial Arrangement of Glycoproteins in the Plasma Membrane
title Glycan Structures Contain Information for the Spatial Arrangement of Glycoproteins in the Plasma Membrane
title_full Glycan Structures Contain Information for the Spatial Arrangement of Glycoproteins in the Plasma Membrane
title_fullStr Glycan Structures Contain Information for the Spatial Arrangement of Glycoproteins in the Plasma Membrane
title_full_unstemmed Glycan Structures Contain Information for the Spatial Arrangement of Glycoproteins in the Plasma Membrane
title_short Glycan Structures Contain Information for the Spatial Arrangement of Glycoproteins in the Plasma Membrane
title_sort glycan structures contain information for the spatial arrangement of glycoproteins in the plasma membrane
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3765438/
https://www.ncbi.nlm.nih.gov/pubmed/24040379
http://dx.doi.org/10.1371/journal.pone.0075013
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