In Vitro Biochemical Assays for O‐GlcNAc‐Processing Enzymes

Kim, Sang Hyun

doi:10.1002/cbic.201700138

Cited by 6 publications

(6 citation statements)

References 105 publications

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“…OGT catalyses an essential post‐transitional modification, the addition of a single GlcNAc onto serine or threonine of nucleocytoplasmic proteins, using UDP‐GlcNAc as donor substrate . OGT is also known to be involved in the processing of the host cell factor C1 (HCF1), the proteolytic products of which are involved in the activation of many genes involved in cell cycle progression . The enzyme is divided into a glycosyltransferase catalytic domain and an N‐terminal domain consisting of 13.5 tetratricopeptide repeats (TPRs) that have been shown to contribute to protein substrate binding .…”

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confidence: 99%

A missense mutation in the catalytic domain of O‐GlcNAc transferase links perturbations in protein O‐GlcNAcylation to X‐linked intellectual disability

et al. 2019

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X‐linked intellectual disabilities (XLID) are common developmental disorders. The enzyme O‐GlcNAc transferase encoded by OGT, a recently discovered XLID gene, attaches O‐GlcNAc to nuclear and cytoplasmic proteins. As few missense mutations have been described, it is unclear what the aetiology of the patient phenotypes is. Here, we report the discovery of a missense mutation in the catalytic domain of OGT in an XLID patient. X‐ray crystallography reveals that this variant leads to structural rearrangements in the catalytic domain. The mutation reduces in vitro OGT activity on substrate peptides/protein. Mouse embryonic stem cells carrying the mutation reveal reduced O‐GlcNAcase (OGA) and global O‐GlcNAc levels. These data suggest a direct link between changes in the O‐GlcNAcome and intellectual disability observed in patients carrying OGT mutations.

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confidence: 99%

A missense mutation in the catalytic domain of O‐GlcNAc transferase links perturbations in protein O‐GlcNAcylation to X‐linked intellectual disability

et al. 2019

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“…Meanwhile, OGA recognizes the specific characteristics of substrate peptides and hydrolyzes GlcNAc from a wide range of peptide sequences [ 119 ]. In addition, some specific residues on OGA contribute to its interaction with different peptide substrates, which means the differential regulation of O -GlcNAcylation on various proteins [ 120 ]. OGA is also affected by PTMs such as phosphorylation and O -GlcNAcylation [ 121 ].…”

Section: Dynamic O -Glcnacylation Cycle and Hexosa...mentioning

confidence: 99%

O-GlcNAcylation: The Underestimated Emerging Regulators of Skeletal Muscle Physiology

Liu

Fan

et al. 2022

Cells

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O-GlcNAcylation is a highly dynamic, reversible and atypical glycosylation that regulates the activity, biological function, stability, sublocation and interaction of target proteins. O-GlcNAcylation receives and coordinates different signal inputs as an intracellular integrator similar to the nutrient sensor and stress receptor, which target multiple substrates with spatio-temporal analysis specifically to maintain cellular homeostasis and normal physiological functions. Our review gives a brief description of O-GlcNAcylation and its only two processing enzymes and HBP flux, which will help to better understand its physiological characteristics of sensing nutrition and environmental cues. This nutritional and stress-sensitive properties of O-GlcNAcylation allow it to participate in the precise regulation of skeletal muscle metabolism. This review discusses the mechanism of O-GlcNAcylation to alleviate metabolic disorders and the controversy about the insulin resistance of skeletal muscle. The level of global O-GlcNAcylation is precisely controlled and maintained in the “optimal zone”, and its abnormal changes is a potential factor in the pathogenesis of cancer, neurodegeneration, diabetes and diabetic complications. Although the essential role of O-GlcNAcylation in skeletal muscle physiology has been widely studied and recognized, it still is underestimated and overlooked. This review highlights the latest progress and potential mechanisms of O-GlcNAcylation in the regulation of skeletal muscle contraction and structural properties.

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“…The longer isoform, full-length OGA, is composed of an N-terminal GlcNAc hydrolytic cleavage domain for the removal of O-GlcNAc from target proteins [28]. Although there is a C-terminal acetyltransferase-like domain that shares sequence homology with GCN5 histone acetyltransferase (HAT) [29,30], there are discrepancies among several reports on the HAT activity of OGA [38,39]. Moreover, since structural analysis indicates that the C-terminal acetyltransferase-like domain lacks essential residues for the binding of acetyl-CoA as a substrate [40], it is likely that the acetyltransferase-like domain has no HAT activity.…”

Section: Regulation Of O-glcnacylationmentioning

confidence: 99%

Histone O-GlcNAcylation and Potential Biological Functions

Hirosawa¹,

Hayakawa²,

Shiota³

et al. 2018

obm genet

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Histone modifications play an important role in the control of DNA-based processes by altering the structure and function of chromatin. O-linked N-acetylglucosamine (O-GlcNAc) modification is a form of post-translational modification of proteins that affects the serine (Ser)/threonine (Thr) residues. This process is controlled by a single pair of enzymes, i.e. O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). Recent evidence indicates the existence of O-GlcNAc modification of histones, with 16 histone O-GlcNAc sites reported to date. O-GlcNAc modification is a nutrient-sensitive modification; therefore, it is likely to serve as a molecular mechanism linking nutrient conditions and epigenetic status. Recently, functional analyses have been advanced by the acquisition of antibodies for the specific detection of O-GlcNAcylation of histone residues. Here, we discuss the current knowledge of histone O-GlcNAc modification, with a view to elucidating its comprehensive biological functions.

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In Vitro Biochemical Assays for O‐GlcNAc‐Processing Enzymes

Cited by 6 publications

References 105 publications

A missense mutation in the catalytic domain of O‐GlcNAc transferase links perturbations in protein O‐GlcNAcylation to X‐linked intellectual disability

A missense mutation in the catalytic domain of O‐GlcNAc transferase links perturbations in protein O‐GlcNAcylation to X‐linked intellectual disability

O-GlcNAcylation: The Underestimated Emerging Regulators of Skeletal Muscle Physiology

Histone O-GlcNAcylation and Potential Biological Functions

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