Detection and analysis of (O-linked β-N-acetylglucosamine)-modified proteins

Natasha E. Zachara

doi:10.1007/978-1-60327-461-6_13

Detection and analysis of (O-linked β-N-acetylglucosamine)-modified proteins

Natasha E. Zachara

School of Medicine

Research output: Chapter in Book/Report/Conference proceeding › Chapter

7 Scopus citations

Abstract

Glycosylation is one of the most common and complex forms of posttranslational modifications of proteins in eukaryotes. Seven different protein-carbohydrate linkages have been characterized on nuclear and cytoplasmic glycoproteins, the most widespread of which is the modification of Ser/Thr residues with monosaccharides of O-linked β-N-acetylglucosamine (O-GlcNAc). O-GlcNAc modification is concentrated in nuclear proteins. O-GlcNAc is thought to regulate protein function in a manner analogous to phosphorylation; and is implicated in the regulation of transcription, the proteasome, insulin and MAP kinase signaling, the cell cycle, and the cellular stress response. In this chapter we focus on methods for the detection of O-GlcNAc-modified proteins and discuss general techniques for the detection and subsequent analysis of other protein-carbohydrate conjugates.

Original language	English (US)
Title of host publication	The Nucleus
Subtitle of host publication	Volume 2: Chromatin, Transcription, Envelope, Proteins, Dynamics, and Imaging
Publisher	Humana Press
Pages	227-254
Number of pages	28
ISBN (Print)	9781603274609
DOIs	https://doi.org/10.1007/978-1-60327-461-6_13
State	Published - 2008

Publication series

Name	Methods in Molecular Biology
Volume	464
ISSN (Print)	1064-3745

Keywords

Affinity purification
Glycomics
Mass spectrometry
O-GlcNAc
Posttranslational modification
Protein glycosylation
Signal transduction
Site-mapping

ASJC Scopus subject areas

Molecular Biology
Genetics

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10.1007/978-1-60327-461-6_13

Cite this

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abstract = "Glycosylation is one of the most common and complex forms of posttranslational modifications of proteins in eukaryotes. Seven different protein-carbohydrate linkages have been characterized on nuclear and cytoplasmic glycoproteins, the most widespread of which is the modification of Ser/Thr residues with monosaccharides of O-linked β-N-acetylglucosamine (O-GlcNAc). O-GlcNAc modification is concentrated in nuclear proteins. O-GlcNAc is thought to regulate protein function in a manner analogous to phosphorylation; and is implicated in the regulation of transcription, the proteasome, insulin and MAP kinase signaling, the cell cycle, and the cellular stress response. In this chapter we focus on methods for the detection of O-GlcNAc-modified proteins and discuss general techniques for the detection and subsequent analysis of other protein-carbohydrate conjugates.",

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N2 - Glycosylation is one of the most common and complex forms of posttranslational modifications of proteins in eukaryotes. Seven different protein-carbohydrate linkages have been characterized on nuclear and cytoplasmic glycoproteins, the most widespread of which is the modification of Ser/Thr residues with monosaccharides of O-linked β-N-acetylglucosamine (O-GlcNAc). O-GlcNAc modification is concentrated in nuclear proteins. O-GlcNAc is thought to regulate protein function in a manner analogous to phosphorylation; and is implicated in the regulation of transcription, the proteasome, insulin and MAP kinase signaling, the cell cycle, and the cellular stress response. In this chapter we focus on methods for the detection of O-GlcNAc-modified proteins and discuss general techniques for the detection and subsequent analysis of other protein-carbohydrate conjugates.

AB - Glycosylation is one of the most common and complex forms of posttranslational modifications of proteins in eukaryotes. Seven different protein-carbohydrate linkages have been characterized on nuclear and cytoplasmic glycoproteins, the most widespread of which is the modification of Ser/Thr residues with monosaccharides of O-linked β-N-acetylglucosamine (O-GlcNAc). O-GlcNAc modification is concentrated in nuclear proteins. O-GlcNAc is thought to regulate protein function in a manner analogous to phosphorylation; and is implicated in the regulation of transcription, the proteasome, insulin and MAP kinase signaling, the cell cycle, and the cellular stress response. In this chapter we focus on methods for the detection of O-GlcNAc-modified proteins and discuss general techniques for the detection and subsequent analysis of other protein-carbohydrate conjugates.

KW - Affinity purification

KW - Glycomics

KW - Mass spectrometry

KW - O-GlcNAc

KW - Posttranslational modification

KW - Protein glycosylation

KW - Signal transduction

KW - Site-mapping

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Detection and analysis of (O-linked β-N-acetylglucosamine)-modified proteins

Abstract

Publication series

Keywords

ASJC Scopus subject areas

Access to Document

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