Regulation of the Inositol 1,4,5-Trisphosphate Receptor Type I by<i>O</i>-GlcNAc Glycosylation

Rengifo, Juliana; Gibson, Craig J.; Winkler, Eva C.; Collin, Thibault; Ehrlich, Barbara E.

doi:10.1523/jneurosci.2069-07.2007

Cited by 39 publications

(46 citation statements)

References 54 publications

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“…The IP 3 type I receptor is the principle intracellular calcium release channel in many cell types including neurons and it is regulated by calcium, ATP, and O-GlcNAc. OGlcNAcylation of the IP 3 type I receptor decreased its activity, while the removal of O-GlcNAc restored its function (Rengifo et al 2007). Following this study, it was demonstrated that the IP 3 type III receptor is functionally regulated by O-GlcNAc, except that O-GlcNAcylation enhanced its activity while O-GlcNAc removal negated its function (Bimboese et al 2011).…”

Section: Calcium Homeostasismentioning

confidence: 77%

“…Following this study, it was demonstrated that the IP 3 type III receptor is functionally regulated by O-GlcNAc, except that O-GlcNAcylation enhanced its activity while O-GlcNAc removal negated its function (Bimboese et al 2011). Thus, O-GlcNAcylation of IP 3 type I and III receptors regulates their function(s) in controlling Ca 2+ flux and ultimately attenuating Ca 2+ -dependent apoptosis (Rengifo et al 2007). …”

Section: Calcium Homeostasismentioning

confidence: 99%

“…O-GlcNAc is thought to regulate these proteins in a manner analogous to protein phosphorylation. O-GlcNAc has been demonstrated to alter numerous protein functions that include: DNA binding and transactivation (Jackson and Tjian 1989;Ozcan et al 2010;Comer and Hart 1999;Gao et al 2003;Sayat et al 2008), protein-protein interactions (Lim and Chang 2010;Ise et al 2010;Guinez et al 2010;Guinez et al 2007;Guinez et al 2006), protein degradation (Cheng and Hart 2001;Han and Kudlow 1997;Zhang et al 2003), protein and enzyme activity Rengifo et al 2007;Zhang et al 2003;Dias et al 2009;Bimboese et al 2011), and protein localization (Sayat et al 2008;Dudognon et al 2004) among many others .…”

mentioning

confidence: 99%

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Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis

Groves

Lee

Yildirir

et al. 2013

Cell Stress and Chaperones

120

112

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O-linked N-acetyl-β-D-glucosamine (O-GlcNAc) is a ubiquitous and dynamic post-translational modification known to modify over 3,000 nuclear, cytoplasmic, and mitochondrial eukaryotic proteins. Addition of O-GlcNAc to proteins is catalyzed by the O-GlcNAc transferase and is removed by a neutral-N-acetyl-β-glucosaminidase (OGlcNAcase). O-GlcNAc is thought to regulate proteins in a manner analogous to protein phosphorylation, and the cycling of this carbohydrate modification regulates many cellular functions such as the cellular stress response. Diverse forms of cellular stress and tissue injury result in enhanced O-GlcNAc modification, or O-GlcNAcylation, of numerous intracellular proteins. Stress-induced OGlcNAcylation appears to promote cell/tissue survival by regulating a multitude of biological processes including: the phosphoinositide 3-kinase/Akt pathway, heat shock protein expression, calcium homeostasis, levels of reactive oxygen species, ER stress, protein stability, mitochondrial dynamics, and inflammation. Here, we will discuss the regulation of these processes by O-GlcNAc and the impact of such regulation on survival in models of ischemia reperfusion injury and trauma hemorrhage. We will also discuss the misregulation of O-GlcNAc in diseases commonly associated with the stress response, namely Alzheimer's and Parkinson's diseases. Finally, we will highlight recent advancements in the tools and technologies used to study the O-GlcNAc modification.

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Section: Calcium Homeostasismentioning

confidence: 77%

Section: Calcium Homeostasismentioning

confidence: 99%

mentioning

confidence: 99%

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Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis

Groves

Lee

Yildirir

et al. 2013

Cell Stress and Chaperones

120

112

View full text Add to dashboard Cite

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“…Unlike other forms of glycosylation in cells that occurs within the secretory pathway, O-GlcNAc modifications occur in the nucleus and cytoplasm [3]. O-GlcNAc glycosylation has been shown to play a role in regulating protein function by influencing enzymatic activity, stability and subcellular localization of proteins [4][5][6][7]. O-GlcNAcylation is sensitive to the nutritional state of the cell as components used for synthesis of uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), the substrate for OGT, are generated from nutrients.…”

Section: Introductionmentioning

confidence: 99%

Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) is regulated by O-GlcNAc transferase

Han

Valdez

et al. 2017

Free Radical Biology and Medicine

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A B S T R A C TThe Nrf1 (Nuclear factor E2-related factor 1) transcription factor performs a critical role in regulating cellular homeostasis. Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1. Nrf1a directly interacts with HCF1 through the HCF1 binding motif (HBM), while interaction with OGT is mediated through HCF1. Overexpression of HCF1 and OGT leads to increased Nrf1a protein stability. Addition of O-GlcNAc decreases ubiquitination and degradation of Nrf1a. Transcriptional activation by Nrf1a is increased by OGT overexpression and treatment with PUGNAc. Together, these data suggest that OGT can act as a regulator of Nrf1a.

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“…A variety of different types of PTMs (e.g., Ubiquitylation, SUMOylation, O-glycosylation/ O-GlcNAcylation, etc.) exist and are discussed elsewhere (14,22,98,99).…”

Section: Introductionmentioning

confidence: 99%

S-Glutathionylation of Ion Channels: Insights into the Regulation of Channel Functions, Thiol Modification Crosstalk, and Mechanosensing

Yang

Jin²,

Jiang³

2014

Antioxidants & Redox Signaling

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Significance: Ion channels control membrane potential, cellular excitability, and Ca ++ signaling, all of which play essential roles in cellular functions. The regulation of ion channels enables cells to respond to changing environments, and post-translational modification (PTM) is one major regulation mechanism. Recent Advances: Many PTMs (e.g., S-glutathionylation, S-nitrosylation, S-palmitoylation, S-sulfhydration, etc.) targeting the thiol group of cysteine residues have emerged to be essential for ion channels regulation under physiological and pathological conditions. Critical Issues: Under oxidative stress, S-glutathionylation could be a critical PTM that regulates many molecules. In this review, we discuss S-glutathionylation-mediated structural and functional changes of ion channels. Criteria for testing S-glutathionylation, methods and reagents used in ion channel S-glutathionylation studies, and thiol modification crosstalk, are also covered. Mechanotransduction, and S-glutathionylation of the mechanosensitive K ATP channel, are discussed. Future Directions: Further investigation of the ion channel S-glutathionylation, especially the physiological significance of S-glutathionylation and thiol modification crosstalk, could lead to a better understanding of the thiol modifications in general and the ramifications of such modifications on cellular functions and related diseases. Antioxid. Redox Signal. 20, 937-951.

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Regulation of the Inositol 1,4,5-Trisphosphate Receptor Type I byO-GlcNAc Glycosylation

Cited by 39 publications

References 54 publications

Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis

Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis

Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) is regulated by O-GlcNAc transferase

S-Glutathionylation of Ion Channels: Insights into the Regulation of Channel Functions, Thiol Modification Crosstalk, and Mechanosensing

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