Potential coordination role between O-GlcNAcylation and epigenetics
Abstract Dynamic changes of the post-translational O-GlcNAc modification (O-GlcNAcylation) are controlled by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) and the glycoside hydrolase O-GlcNAcase (OGA) in cells. O-GlcNAcylation often occurs on serine (Ser) and threonine (Thr) residues o...
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| Format: | Article |
| Language: | English |
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Oxford University Press
2017-05-01
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| Series: | Protein & Cell |
| Subjects: | |
| Online Access: | http://link.springer.com/article/10.1007/s13238-017-0416-4 |
| _version_ | 1827836585957130240 |
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| author | Donglu Wu Yong Cai Jingji Jin |
| author_facet | Donglu Wu Yong Cai Jingji Jin |
| author_sort | Donglu Wu |
| collection | DOAJ |
| description | Abstract Dynamic changes of the post-translational O-GlcNAc modification (O-GlcNAcylation) are controlled by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) and the glycoside hydrolase O-GlcNAcase (OGA) in cells. O-GlcNAcylation often occurs on serine (Ser) and threonine (Thr) residues of the specific substrate proteins via the addition of O-GlcNAc group by OGT. It has been known that O-GlcNAcylation is not only involved in many fundamental cellular processes, but also plays an important role in cancer development through various mechanisms. Recently, accumulating data reveal that O-GlcNAcylation at histones or non-histone proteins can lead to the start of the subsequent biological processes, suggesting that O-GlcNAcylation as ‘protein code’ or ‘histone code’ may provide recognition platforms or executive instructions for subsequent recruitment of proteins to carry out the specific functions. In this review, we summarize the interaction of O-GlcNAcylation and epigenetic changes, introduce recent research findings that link crosstalk between O-GlcNAcylation and epigenetic changes, and speculate on the potential coordination role of O-GlcNAcylation with epigenetic changes in intracellular biological processes. |
| first_indexed | 2024-03-12T06:28:56Z |
| format | Article |
| id | doaj.art-5caca5c104a94285a02274904dec74fb |
| institution | Directory Open Access Journal |
| issn | 1674-800X 1674-8018 |
| language | English |
| last_indexed | 2024-03-12T06:28:56Z |
| publishDate | 2017-05-01 |
| publisher | Oxford University Press |
| record_format | Article |
| series | Protein & Cell |
| spelling | doaj.art-5caca5c104a94285a02274904dec74fb2023-09-03T01:43:14ZengOxford University PressProtein & Cell1674-800X1674-80182017-05-0181071372310.1007/s13238-017-0416-4Potential coordination role between O-GlcNAcylation and epigeneticsDonglu Wu0Yong Cai1Jingji Jin2School of Life Sciences, Jilin UniversitySchool of Life Sciences, Jilin UniversitySchool of Life Sciences, Jilin UniversityAbstract Dynamic changes of the post-translational O-GlcNAc modification (O-GlcNAcylation) are controlled by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) and the glycoside hydrolase O-GlcNAcase (OGA) in cells. O-GlcNAcylation often occurs on serine (Ser) and threonine (Thr) residues of the specific substrate proteins via the addition of O-GlcNAc group by OGT. It has been known that O-GlcNAcylation is not only involved in many fundamental cellular processes, but also plays an important role in cancer development through various mechanisms. Recently, accumulating data reveal that O-GlcNAcylation at histones or non-histone proteins can lead to the start of the subsequent biological processes, suggesting that O-GlcNAcylation as ‘protein code’ or ‘histone code’ may provide recognition platforms or executive instructions for subsequent recruitment of proteins to carry out the specific functions. In this review, we summarize the interaction of O-GlcNAcylation and epigenetic changes, introduce recent research findings that link crosstalk between O-GlcNAcylation and epigenetic changes, and speculate on the potential coordination role of O-GlcNAcylation with epigenetic changes in intracellular biological processes.http://link.springer.com/article/10.1007/s13238-017-0416-4O-GlcNAcylationpost-translational modificationhistone modificationepigenetics |
| spellingShingle | Donglu Wu Yong Cai Jingji Jin Potential coordination role between O-GlcNAcylation and epigenetics Protein & Cell O-GlcNAcylation post-translational modification histone modification epigenetics |
| title | Potential coordination role between O-GlcNAcylation and epigenetics |
| title_full | Potential coordination role between O-GlcNAcylation and epigenetics |
| title_fullStr | Potential coordination role between O-GlcNAcylation and epigenetics |
| title_full_unstemmed | Potential coordination role between O-GlcNAcylation and epigenetics |
| title_short | Potential coordination role between O-GlcNAcylation and epigenetics |
| title_sort | potential coordination role between o glcnacylation and epigenetics |
| topic | O-GlcNAcylation post-translational modification histone modification epigenetics |
| url | http://link.springer.com/article/10.1007/s13238-017-0416-4 |
| work_keys_str_mv | AT dongluwu potentialcoordinationrolebetweenoglcnacylationandepigenetics AT yongcai potentialcoordinationrolebetweenoglcnacylationandepigenetics AT jingjijin potentialcoordinationrolebetweenoglcnacylationandepigenetics |