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Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc
Abstract
The dynamic glycosylation of serine or threonine residues on nuclear and cytosolic proteins by O-linked β- N -acetylglucosamine (O-GlcNAc) is abundant in all multicellular eukaryotes. On several proteins, O-GlcNAc and O-phosphate alternatively occupy the same or adjacent sites, leading to the hypothesis that one function of this saccharide is to transiently block phosphorylation. The diversity of proteins modified by O-GlcNAc implies its importance in many basic cellular and disease processes. Here we systematically examine the current data implicating O-GlcNAc as a regulatory modification important to signal transduction cascades.
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Cited by
Prescher, J. A., & Bertozzi, C. R. (2005) · Nature Chemical Biology · doi:10.1038/nchembio0605-13 · Cited by 1,456
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-citationHart, G. W., Slawson, C., Ramirez-Correa, G., & Lagerlof, O. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060608-102511 · Cited by 1,317
Self-citationShimura, H., Schlossmacher, M. G., Hattori, N., Frosch, M. P., Trockenbacher, A., Schneider, R., Mizuno, Y., Kosik, K. S., & Selkoe, D. J. (2001) · Science · doi:10.1126/science.1060627 · Cited by 1,053
Global Analysis of DELLA Direct Targets in Early Gibberellin Signaling in Arabidopsis
Zentella, R., Zhang, Z.-L., Park, M., Thomas, S. G., Endo, A., Murase, K., Fleet, C. M., Jikumaru, Y., Nambara, E., Kamiya, Y., et al. (2007) · The Plant Cell · doi:10.1105/tpc.107.054999 · Cited by 678
Metadata
- Authors
- Wells, L., Vosseller, K., & Hart, G. W.
- Venue
- Science
- Published
- 2001-03-23
- Volume
- 291
- Issue
- 5512
- Pages
- 2376-2378
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2085677500
- Cited by
- 954
- References
- 0
- FWCI
- 22.26
- Type
- journal article
- Language
- en
- Open access
- closed
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