Analytical Technologies for Identification and Characterization of the Plant N-Glycoproteome
N-glycosylation is one of the most common and complex post-translational modifications of eukaryotic proteins and one that has numerous roles, such as modulating protein stability, sorting, folding, enzyme activity and ligand interactions. In plants, the functional significance of N-glycosylation is...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2012-07-01
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| Series: | Frontiers in Plant Science |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fpls.2012.00150/full |
| _version_ | 1811254299014987776 |
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| author | Eliel eRuiz-May Theodore William Thannhauser Sheng eZhang Jocelyn Kenneth Campbell Rose |
| author_facet | Eliel eRuiz-May Theodore William Thannhauser Sheng eZhang Jocelyn Kenneth Campbell Rose |
| author_sort | Eliel eRuiz-May |
| collection | DOAJ |
| description | N-glycosylation is one of the most common and complex post-translational modifications of eukaryotic proteins and one that has numerous roles, such as modulating protein stability, sorting, folding, enzyme activity and ligand interactions. In plants, the functional significance of N-glycosylation is typically obscure, although it is a feature of most secreted proteins and so is potentially of considerable interest to plant cell wall biologists. While analytical pipelines have been established to characterize yeast, mammalian and bacterial N-glycoproteomes, such large-scale approaches for the study of plant glycoproteins have yet to be reported. Indeed, the N-glycans that decorate plant and mammalian or yeast proteins are structurally distinct and so modification of existing analytical approaches are needed to tackle plant N-glycoproteomes. In this review, we summarize a range of existing technologies for large-scale N-glycoprotein analysis and highlight promising future approaches that may provide a better understanding of the plant N-glycoproteome, and therefore the cell wall proteome and other proteins associated with the secretory pathway. |
| first_indexed | 2024-04-12T17:05:15Z |
| format | Article |
| id | doaj.art-6195cc3467a64a0a8e888cbb2128a1b7 |
| institution | Directory Open Access Journal |
| issn | 1664-462X |
| language | English |
| last_indexed | 2024-04-12T17:05:15Z |
| publishDate | 2012-07-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Plant Science |
| spelling | doaj.art-6195cc3467a64a0a8e888cbb2128a1b72022-12-22T03:23:58ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2012-07-01310.3389/fpls.2012.0015026658Analytical Technologies for Identification and Characterization of the Plant N-GlycoproteomeEliel eRuiz-May0Theodore William Thannhauser1Sheng eZhang2Jocelyn Kenneth Campbell Rose3Cornell UniversityUSDA-ARSCornell UniversityCornell UniversityN-glycosylation is one of the most common and complex post-translational modifications of eukaryotic proteins and one that has numerous roles, such as modulating protein stability, sorting, folding, enzyme activity and ligand interactions. In plants, the functional significance of N-glycosylation is typically obscure, although it is a feature of most secreted proteins and so is potentially of considerable interest to plant cell wall biologists. While analytical pipelines have been established to characterize yeast, mammalian and bacterial N-glycoproteomes, such large-scale approaches for the study of plant glycoproteins have yet to be reported. Indeed, the N-glycans that decorate plant and mammalian or yeast proteins are structurally distinct and so modification of existing analytical approaches are needed to tackle plant N-glycoproteomes. In this review, we summarize a range of existing technologies for large-scale N-glycoprotein analysis and highlight promising future approaches that may provide a better understanding of the plant N-glycoproteome, and therefore the cell wall proteome and other proteins associated with the secretory pathway.http://journal.frontiersin.org/Journal/10.3389/fpls.2012.00150/fullMass SpectrometryplantglycoproteinN-glycanLectin |
| spellingShingle | Eliel eRuiz-May Theodore William Thannhauser Sheng eZhang Jocelyn Kenneth Campbell Rose Analytical Technologies for Identification and Characterization of the Plant N-Glycoproteome Frontiers in Plant Science Mass Spectrometry plant glycoprotein N-glycan Lectin |
| title | Analytical Technologies for Identification and Characterization of the Plant N-Glycoproteome |
| title_full | Analytical Technologies for Identification and Characterization of the Plant N-Glycoproteome |
| title_fullStr | Analytical Technologies for Identification and Characterization of the Plant N-Glycoproteome |
| title_full_unstemmed | Analytical Technologies for Identification and Characterization of the Plant N-Glycoproteome |
| title_short | Analytical Technologies for Identification and Characterization of the Plant N-Glycoproteome |
| title_sort | analytical technologies for identification and characterization of the plant n glycoproteome |
| topic | Mass Spectrometry plant glycoprotein N-glycan Lectin |
| url | http://journal.frontiersin.org/Journal/10.3389/fpls.2012.00150/full |
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