O-GlcNAcylation and its role in the immune system
Abstract O-linked-N-acetylglucosaminylation (O-GlcNAcylation) is a type of glycosylation that occurs when a monosaccharide, O-GlcNAc, is added onto serine or threonine residues of nuclear or cytoplasmic proteins by O-GlcNAc transferase (OGT) and which can be reversibly removed by O-GlcNAcase (OGA)....
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| Format: | Article |
| Language: | English |
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BMC
2020-04-01
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| Series: | Journal of Biomedical Science |
| Subjects: | |
| Online Access: | http://link.springer.com/article/10.1186/s12929-020-00648-9 |
| _version_ | 1819099532908036096 |
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| author | Yi-Hsuan Chang Chia-Lin Weng Kuo-I Lin |
| author_facet | Yi-Hsuan Chang Chia-Lin Weng Kuo-I Lin |
| author_sort | Yi-Hsuan Chang |
| collection | DOAJ |
| description | Abstract O-linked-N-acetylglucosaminylation (O-GlcNAcylation) is a type of glycosylation that occurs when a monosaccharide, O-GlcNAc, is added onto serine or threonine residues of nuclear or cytoplasmic proteins by O-GlcNAc transferase (OGT) and which can be reversibly removed by O-GlcNAcase (OGA). O-GlcNAcylation couples the processes of nutrient sensing, metabolism, signal transduction and transcription, and plays important roles in development, normal physiology and physiopathology. Cumulative studies have indicated that O-GlcNAcylation affects the functions of protein substrates in a number of ways, including protein cellular localization, protein stability and protein/protein interaction. Particularly, O-GlcNAcylation has been shown to have intricate crosstalk with phosphorylation as they both modify serine or threonine residues. Aberrant O-GlcNAcylation on various protein substrates has been implicated in many diseases, including neurodegenerative diseases, diabetes and cancers. However, the role of protein O-GlcNAcylation in immune cell lineages has been less explored. This review summarizes the current understanding of the fundamental biochemistry of O-GlcNAcylation, and discusses the molecular mechanisms by which O-GlcNAcylation regulates the development, maturation and functions of immune cells. In brief, O-GlcNAcylation promotes the development, proliferation, and activation of T and B cells. O-GlcNAcylation regulates inflammatory and antiviral responses of macrophages. O-GlcNAcylation promotes the function of activated neutrophils, but inhibits the activity of nature killer cells. |
| first_indexed | 2024-12-22T00:48:23Z |
| format | Article |
| id | doaj.art-e4f076185db2495199e2ba353a2bb2c8 |
| institution | Directory Open Access Journal |
| issn | 1423-0127 |
| language | English |
| last_indexed | 2024-12-22T00:48:23Z |
| publishDate | 2020-04-01 |
| publisher | BMC |
| record_format | Article |
| series | Journal of Biomedical Science |
| spelling | doaj.art-e4f076185db2495199e2ba353a2bb2c82022-12-21T18:44:30ZengBMCJournal of Biomedical Science1423-01272020-04-0127111510.1186/s12929-020-00648-9O-GlcNAcylation and its role in the immune systemYi-Hsuan Chang0Chia-Lin Weng1Kuo-I Lin2Genomics Research Center, Academia SinicaGenomics Research Center, Academia SinicaGenomics Research Center, Academia SinicaAbstract O-linked-N-acetylglucosaminylation (O-GlcNAcylation) is a type of glycosylation that occurs when a monosaccharide, O-GlcNAc, is added onto serine or threonine residues of nuclear or cytoplasmic proteins by O-GlcNAc transferase (OGT) and which can be reversibly removed by O-GlcNAcase (OGA). O-GlcNAcylation couples the processes of nutrient sensing, metabolism, signal transduction and transcription, and plays important roles in development, normal physiology and physiopathology. Cumulative studies have indicated that O-GlcNAcylation affects the functions of protein substrates in a number of ways, including protein cellular localization, protein stability and protein/protein interaction. Particularly, O-GlcNAcylation has been shown to have intricate crosstalk with phosphorylation as they both modify serine or threonine residues. Aberrant O-GlcNAcylation on various protein substrates has been implicated in many diseases, including neurodegenerative diseases, diabetes and cancers. However, the role of protein O-GlcNAcylation in immune cell lineages has been less explored. This review summarizes the current understanding of the fundamental biochemistry of O-GlcNAcylation, and discusses the molecular mechanisms by which O-GlcNAcylation regulates the development, maturation and functions of immune cells. In brief, O-GlcNAcylation promotes the development, proliferation, and activation of T and B cells. O-GlcNAcylation regulates inflammatory and antiviral responses of macrophages. O-GlcNAcylation promotes the function of activated neutrophils, but inhibits the activity of nature killer cells.http://link.springer.com/article/10.1186/s12929-020-00648-9O-GlcNAcylationOGTOGAImmune cells |
| spellingShingle | Yi-Hsuan Chang Chia-Lin Weng Kuo-I Lin O-GlcNAcylation and its role in the immune system Journal of Biomedical Science O-GlcNAcylation OGT OGA Immune cells |
| title | O-GlcNAcylation and its role in the immune system |
| title_full | O-GlcNAcylation and its role in the immune system |
| title_fullStr | O-GlcNAcylation and its role in the immune system |
| title_full_unstemmed | O-GlcNAcylation and its role in the immune system |
| title_short | O-GlcNAcylation and its role in the immune system |
| title_sort | o glcnacylation and its role in the immune system |
| topic | O-GlcNAcylation OGT OGA Immune cells |
| url | http://link.springer.com/article/10.1186/s12929-020-00648-9 |
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