Location and characterization of the O-GlcNAcase active site

Toleman, Clifford A.; Paterson, Andrew J.; Kudlow, Jeffrey E.

doi:10.1016/j.bbagen.2006.01.017

Cited by 24 publications

(34 citation statements)

References 50 publications

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“…O-GlcNAcase Assay-O-GlcNAcase activity was determined, with some modifications, as described previously using 4-methylumbelliferyl GlcNAc as substrate (36,37). Cell extracts (25 l) prepared in isotonic buffer (20 mM Tris-HCl, pH 7.5, 10% glycerol) were added to 250 M 4-methylumbelliferyl GlcNAc and 50 mM N-acetylgalactosamine in 50 mM NaH 2 PO 4 , 100 mM NaCl, pH 6.4, reaction buffer in a total volume of 50 l. Assays were carried out at 37°C for 30 min, and the reaction was quenched by the addition of 300 l of sodium hydroxide-buffered 0.2 M glycine, pH 10.75.…”

Section: Methodsmentioning

confidence: 99%

Glucose Deprivation-induced Increase in Protein O-GlcNAcylation in Cardiomyocytes Is Calcium-dependent

Zou

Zhu-Mauldin

Marchase

et al. 2012

Journal of Biological Chemistry

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Background: Levels of cellular protein O-GlcNAc modification increase in response to stress, but mechanism not understood. Results: Glucose deprivation and heat shock-induced increase in O-GlcNAcylation are attenuated by CaMKII inhibition. Conclusion: CaMKII activation plays a key role in regulating the stress-induced increase in O-GlcNAc. Significance: Understanding the regulation of O-GlcNAcylation is critical in determining its role in cellular stress responses.

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Section: Methodsmentioning

confidence: 99%

Glucose Deprivation-induced Increase in Protein O-GlcNAcylation in Cardiomyocytes Is Calcium-dependent

Zou

Zhu-Mauldin

Marchase

et al. 2012

Journal of Biological Chemistry

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“…Cloning of NCOAT variants was previously described (25)(26)(27). The Gal4-tagged NCOAT was previously described (29).…”

Section: Methodsmentioning

confidence: 99%

“…The O-GlcNAcase activity assay was performed as previously described (25). Histone acetyltransferase activity was measured using the previously described "filter paper method" (26).…”

Section: Methodsmentioning

confidence: 99%

“…This interaction appears to target OGT, and thus O-GlcNAc modification, to sites of transcriptional repression (32). The removal of OGlcNAc residues is catalyzed by the enzyme NCOAT (nuclear and cytoplasmic O-GlcNAcase and acetyltransferase; meningioma 5 or MGEA5; O-GlcNAcase), which is the only known protein bearing O-GlcNAcase (OGN) activity, in addition to containing a functional histone acetyltransferase (HAT) domain (25,26). Thus, OGN activity by NCOAT is essential to relieve the effects of O-GlcNAc modification on proteins.…”

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confidence: 99%

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O-GlcNAc Integrates the Proteasome and Transcriptome To Regulate Nuclear Hormone Receptors

Bowe

Sadlonova

Toleman

et al. 2006

Molecular and Cellular Biology

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“…O-GlcNAcase is a 106-kDa heterodimer complex containing a 54-kDa ␣-subunit and a 51-kDa ␤-subunit (48). The catalytic domain of O-GlcNAcase is in the NH 2 -terminus (193), whereas the COOH-terminus has histone acetyl-transferase (HAT) activity in vitro (194). OGlcNAcase contains a caspase-3 cleavage site; thus, it may be regulated during apoptosis (18).…”

Section: Regulation Of Protein O-glcnacylationmentioning

confidence: 99%

ProteinO-GlcNAcylation: a new signaling paradigm for the cardiovascular system

Laczy¹,

Hill²,

Wang³

et al. 2009

American Journal of Physiology-Heart and Circulatory Physiology

141

135

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The posttranslational modification of serine and threonine residues of nuclear and cytoplasmic proteins by the O-linked attachment of the monosaccharide ␤-N-acetylglucosamine (O-GlcNAc) is a highly dynamic and ubiquitous protein modification. Protein O-GlcNAcylation is rapidly emerging as a key regulator of critical biological processes including nuclear transport, translation and transcription, signal transduction, cytoskeletal reorganization, proteasomal degradation, and apoptosis. Increased levels of O-GlcNAc have been implicated as a pathogenic contributor to glucose toxicity and insulin resistance, which are both major hallmarks of diabetes mellitus and diabetes-related cardiovascular complications. Conversely, there is a growing body of data demonstrating that the acute activation of O-GlcNAc levels is an endogenous stress response designed to enhance cell survival. Reports on the effect of altered O-GlcNAc levels on the heart and cardiovascular system have been growing rapidly over the past few years and have implicated a role for O-GlcNAc in contributing to the adverse effects of diabetes on cardiovascular function as well as mediating the response to ischemic injury. Here, we summarize our present understanding of protein O-GlcNAcylation and its effect on the regulation of cardiovascular function. We examine the pathways regulating protein O-GlcNAcylation and discuss, in more detail, our understanding of the role of O-GlcNAc in both mediating the adverse effects of diabetes as well as its role in mediating cellular protective mechanisms in the cardiovascular system. In addition, we also explore the parallels between O-GlcNAc signaling and redox signaling, as an alternative paradigm for understanding the role of O-GlcNAcylation in regulating cell function. hexosamine biosynthesis; protein O-glycosylation; ␤-N-acetylglucosamine transferase; diabetes mellitus POSTTRANSLATIONAL MODIFICATION (PTM) of proteins is a common mechanism for the modulation of protein function, location, and turnover. Although protein phosphorylation is probably the most widely studied form of PTM, there are many other PTMs, including acylation, ubiquitylation, methylation, acetylation, thiolation, nitration, and glycosylation (107). The focus of this review is protein glycosylation, specifically, O-glycosylation of nuclear and cytoplasmic proteins. Classical protein glycosylation occurs in the endoplasmic reticulum and Golgi, leading to the formation of stable and complex elongated oligosaccharide structures via both N-linkage on asparagine and O-linkage on the hydroxy amino acids serine and threonine in addition to hydroxyproline, hydroxylysine, and tyrosine residues of proteins that become secreted or membrane component glycoproteins (189). In contrast, glycosylation of nuclear and cytoplasmic proteins is a rapid and dynamic modification of serine or threonine residues by the O-linked attachment of the monosaccharide ␤-N-acetylglucosamine (OGlcNAc) (97,195); this process is referred to as protein O-GlcNAcylation to contrast it wi...

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Location and characterization of the O-GlcNAcase active site

Cited by 24 publications

References 50 publications

Glucose Deprivation-induced Increase in Protein O-GlcNAcylation in Cardiomyocytes Is Calcium-dependent

Glucose Deprivation-induced Increase in Protein O-GlcNAcylation in Cardiomyocytes Is Calcium-dependent

O-GlcNAc Integrates the Proteasome and Transcriptome To Regulate Nuclear Hormone Receptors

ProteinO-GlcNAcylation: a new signaling paradigm for the cardiovascular system

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