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P-Type Lectins: Cation-Dependent Mannose-6-Phosphate Receptor
In eukaryotic cells, post-translational modification of secreted proteins and intracellular protein transport between organelles are ubiquitous features. One of the most studied systems is the N-linked glycosylation pathway in the synthesis of secreted glycoproteins (Schrag et al. 2003). The N-linke...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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2012
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7121444/ http://dx.doi.org/10.1007/978-3-7091-1065-2_3 |
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author | Gupta, G. S. |
author_facet | Gupta, G. S. |
author_sort | Gupta, G. S. |
collection | PubMed |
description | In eukaryotic cells, post-translational modification of secreted proteins and intracellular protein transport between organelles are ubiquitous features. One of the most studied systems is the N-linked glycosylation pathway in the synthesis of secreted glycoproteins (Schrag et al. 2003). The N-linked glycoproteins are subjected to diverse modifications and are transported through ER and Golgi apparatus to their final destinations in- and outside the cell. Incorporation of cargo glycoproteins into transport vesicles is mediated by transmembrane cargo receptors, which have been identified as intracellular lectins. For example, mannose 6-phosphate receptors (Ghosh et al. 2003) function as a cargo receptor for lysosomal proteins in the trans-Golgi network, whereas ERGIC-53 (Zhang et al. 2003) and its yeast orthologs Emp46/47p (Sato and Nakano 2002) are transport lectins for glycoproteins that are transported out of ER. |
format | Online Article Text |
id | pubmed-7121444 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
record_format | MEDLINE/PubMed |
spelling | pubmed-71214442020-04-06 P-Type Lectins: Cation-Dependent Mannose-6-Phosphate Receptor Gupta, G. S. Animal Lectins: Form, Function and Clinical Applications Article In eukaryotic cells, post-translational modification of secreted proteins and intracellular protein transport between organelles are ubiquitous features. One of the most studied systems is the N-linked glycosylation pathway in the synthesis of secreted glycoproteins (Schrag et al. 2003). The N-linked glycoproteins are subjected to diverse modifications and are transported through ER and Golgi apparatus to their final destinations in- and outside the cell. Incorporation of cargo glycoproteins into transport vesicles is mediated by transmembrane cargo receptors, which have been identified as intracellular lectins. For example, mannose 6-phosphate receptors (Ghosh et al. 2003) function as a cargo receptor for lysosomal proteins in the trans-Golgi network, whereas ERGIC-53 (Zhang et al. 2003) and its yeast orthologs Emp46/47p (Sato and Nakano 2002) are transport lectins for glycoproteins that are transported out of ER. 2012-03-20 /pmc/articles/PMC7121444/ http://dx.doi.org/10.1007/978-3-7091-1065-2_3 Text en © Springer-Verlag Wien 2012 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Article Gupta, G. S. P-Type Lectins: Cation-Dependent Mannose-6-Phosphate Receptor |
title | P-Type Lectins: Cation-Dependent Mannose-6-Phosphate Receptor |
title_full | P-Type Lectins: Cation-Dependent Mannose-6-Phosphate Receptor |
title_fullStr | P-Type Lectins: Cation-Dependent Mannose-6-Phosphate Receptor |
title_full_unstemmed | P-Type Lectins: Cation-Dependent Mannose-6-Phosphate Receptor |
title_short | P-Type Lectins: Cation-Dependent Mannose-6-Phosphate Receptor |
title_sort | p-type lectins: cation-dependent mannose-6-phosphate receptor |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7121444/ http://dx.doi.org/10.1007/978-3-7091-1065-2_3 |
work_keys_str_mv | AT guptags ptypelectinscationdependentmannose6phosphatereceptor |