The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.
β- N -acetylglucosamine (O-GlcNAc) is part of the histone code
Open accessAbstract
Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β- N -acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein–protein interactions. Like phosphorylation, O-GlcNAc cycles in response to a wide variety of stimuli. Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and β- N -acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits. Here, we demonstrate by multiple specific immunological and enzymatic approaches that histones, the proteins that package DNA within the nucleus, are O-GlcNAcylated in vivo. Histones also are substrates for OGT in vitro. We identify O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrometry. Finally, we show that histone O-GlcNAcylation changes during mitosis and with heat shock. Taken together, these data show that O-GlcNAc cycles dynamically on histones and can be considered part of the histone code.
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Cites
2 retracted
GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis
Fujiki, R., Chikanishi, T., Hashiba, W., Ito, H., Takada, I., Roeder, R. G., Kitagawa, H., & Kato, S. (2009) · Nature · doi:10.1038/nature07954 · Cited by 168
RetractedTAF1 Activates Transcription by Phosphorylation of Serine 33 in Histone H2B
Maile, T. M., Kwoczynski, S., Katzenberger, R. J., Wassarman, D. A., & Sauer, F. (2004) · Science · doi:10.1126/science.1095001 · Cited by 69
RetractedCrystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
The Role of Chromatin during Transcription
Li, B., Carey, M., & Workman, J. L. (2007) · Cell · doi:10.1016/j.cell.2007.01.015 · Cited by 3,533
Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., & Mann, M. (2006) · Cell · doi:10.1016/j.cell.2006.09.026 · Cited by 3,499
Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
Hart, G. W., Housley, M. P., & Slawson, C. (2007) · Nature · doi:10.1038/nature05815 · Cited by 1,418
Self-citationTorres, C. R., & Hart, G. W. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43295-9 · Cited by 1,131
Self-citationExtraction, purification and analysis of histones
Shechter, D., Dormann, H. L., Allis, C. D., & Hake, S. B. (2007) · Nature Protocols · doi:10.1038/nprot.2007.202 · Cited by 1,064
Marshall, S., Bacote, V, & Traxinger, R. R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67706-9 · Cited by 1,047
Multivalent engagement of chromatin modifications by linked binding modules
Ruthenburg, A. J., Li, H., Patel, D. J., & David Allis, C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2298 · Cited by 1,013
Cited by
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
Tan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902
Regulation of nucleosome dynamics by histone modifications
Zentner, G. E., & Henikoff, S. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2470 · Cited by 923
Lysine succinylation and lysine malonylation in histones
Xie, Z., Dai, J., Dai, L., Tan, M., Cheng, Z., Wu, Y., Boeke, J. D., & Zhao, Y. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.015875 · Cited by 613
Interplay between Metabolism and Epigenetics: A Nuclear Adaptation to Environmental Changes
Etchegaray, J.-P., & Mostoslavsky, R. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.029 · Cited by 518
Metadata
- Authors
- Sakabe, K., Wang, Z., & Hart, G. W.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2010-11-02
- Volume
- 107
- Issue
- 46
- Pages
- 19915-19920
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2071520055
- Cited by
- 373
- References
- 60
- FWCI
- 9.92
- Type
- journal article
- Language
- en
- Open access
- green
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- Sakabe, K., Wang, Z., & Hart, G. W. (2010). β- N -acetylglucosamine (O-GlcNAc) is part of the histone code. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1009023107
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