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Accepted (AM)Open Access (License Unspecified), Open
Journal article
Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics
Nature chemical biology, v 3(6), pp 339-348
Jun 2007
PMID: 17496889
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The addition of the monosaccharide beta-N-acetyl-D-glucosamine to proteins (O-GlcNAc glycosylation) is an intracellular, post-translational modification that shares features with phosphorylation. Understanding the cellular mechanisms and signaling pathways that regulate O-GlcNAc glycosylation has been challenging because of the difficulty of detecting and quantifying the modification. Here, we describe a new strategy for monitoring the dynamics of O-GlcNAc glycosylation using quantitative mass spectrometry-based proteomics. Our method, which we have termed quantitative isotopic and chemoenzymatic tagging (QUIC-Tag), combines selective, chemoenzymatic tagging of O-GlcNAc proteins with an efficient isotopic labeling strategy. Using the method, we detect changes in O-GlcNAc glycosylation on several proteins involved in the regulation of transcription and mRNA translocation. We also provide the first evidence that O-GlcNAc glycosylation is dynamically modulated by excitatory stimulation of the brain in vivo. Finally, we use electron-transfer dissociation mass spectrometry to identify exact sites of O-GlcNAc modification. Together, our studies suggest that O-GlcNAc glycosylation occurs reversibly in neurons and, akin to phosphorylation, may have important roles in mediating the communication between neurons.
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Details
- Title
- Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics
- Creators
- Nelly Khidekel - California Institute of TechnologyScott B Ficarro - Genomics Institute of the Novartis Research FoundationPeter M Clark - Howard Hughes Medical InstituteMarian C Bryan - Howard Hughes Medical InstituteDanielle L Swaney - University of Wisconsin–MadisonJessica E Rexach - University of California, Los AngelesYi E Sun - University of California, Los AngelesJoshua J Coon - University of Wisconsin–MadisonEric C Peters - Genomics Institute of the Novartis Research FoundationLinda C Hsieh-Wilson - Howard Hughes Medical Institute
- Publication Details
- Nature chemical biology, v 3(6), pp 339-348
- Publisher
- Springer Nature
- Grant note
- R01 NS045061 / NINDS NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- School of Biomedical Engineering, Science, and Health Systems; Drexel University
- Web of Science ID
- WOS:000246816400013
- Scopus ID
- 2-s2.0-34249032767
- Other Identifier
- 991019356341704721
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- Collaboration types
- Industry collaboration
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology