FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W3167574390> ?p ?o ?g. }

• W3167574390 abstract "Mitochondrial dysfunction is a common characteristic of many diseases, such as Alzheimer's disease, diabetes, and cancer. Normal mitochondrial and cellular function is regulated by post-translational modifications (PTM) of proteins, which alter protein function to adapt to changes in the cellular environment. One PTM that plays a key role in protein function is the attachment of a single N-acetylglucosamine (O-GlcNAc) sugar to nuclear, mitochondrial, or cytoplasmic proteins at their serine or threonine residues. This process, known as O-GlcNAcylation, is catalyzed by only two enzymes: O-GlcNAc transferase (OGT), which attaches the sugar, and O-GlcNAcase (OGA), which removes the sugar. O-GlcNAcylation is sensitive to changes in various metabolic pathways, such as the metabolism of glucose, fatty acids, and amino acids. Thus, this modification is necessary for maintaining cellular homeostasis. Our previous data showed that changes in O-GlcNAcylation, such as loss of OGT or inhibition of OGA via thiamet-G (TMG) treatment in the liver, showed disruption of the electron transport chain (ETC); however, we still do not know which complexes are most affected by these changes. One potential explanation lies in the relationship between O-GlcNAcylation and acetylation, as acetylation is a highly abundant mitochondrial PTM responsible for the regulation of many components of the ETC. A variety of cell line knockouts and animal models were studied to more fully understand the role of O-GlcNAcylation in regulating mitochondrial function and acetylation. We generated a stable cell line in SH-SY5Y human neuroblastoma cells with shRNA mediated knockdown of OGT. These cells demonstrated an increase in acetylation in the mitochondria as a result of the loss of OGT. Further analysis also showed changes in the expressions of two proteins that are critical for mitochondrial acetylation: acetyl-coenzyme A synthetase 2-like (ACSS1) and NAD-dependent deacetylase sirtuin-3 (SIRT3). Taken together, these findings suggest that reduced O-GlcNAcylation alters the mitochondrial proteome including proteins that are regulated via acetylation. We also observed that oxidative phosphorylation rates were altered in the OGT knockdown cell lines, demonstrating alterations in mitochondrial function due to the reduction of OGT. To further elucidate the role of O-GlcNAcylation in the electron transport chain, ETC complex assays were run to assess changes in complex function due to different levels of O-GlcNAcylation. SH-SY5Y cells treated with and without TMG expressed different levels of complex activity, providing key insights about the importance of O-GlcNAcylation in the ETC. Based on these findings, more studies are needed to understand how O-GlcNAcylation and acetylation work in tandem to maintain electron transport chain function." @default.
• W3167574390 created "2021-06-22" @default.
• W3167574390 creator A5035406667 @default.
• W3167574390 creator A5044548008 @default.
• W3167574390 creator A5050249978 @default.
• W3167574390 creator A5079568106 @default.
• W3167574390 date "2021-05-01" @default.
• W3167574390 modified "2023-09-26" @default.
• W3167574390 title "Changes in O‐GlcNAcylation Alter Mitochondrial Function" @default.
• W3167574390 doi "https://doi.org/10.1096/fasebj.2021.35.s1.04611" @default.
• W3167574390 hasPublicationYear "2021" @default.
• W3167574390 type Work @default.
• W3167574390 sameAs 3167574390 @default.
• W3167574390 citedByCount "0" @default.
• W3167574390 crossrefType "journal-article" @default.
• W3167574390 hasAuthorship W3167574390A5035406667 @default.
• W3167574390 hasAuthorship W3167574390A5044548008 @default.
• W3167574390 hasAuthorship W3167574390A5050249978 @default.
• W3167574390 hasAuthorship W3167574390A5079568106 @default.
• W3167574390 hasConcept C104317684 @default.
• W3167574390 hasConcept C119157956 @default.
• W3167574390 hasConcept C11960822 @default.
• W3167574390 hasConcept C14036430 @default.
• W3167574390 hasConcept C173396325 @default.
• W3167574390 hasConcept C181199279 @default.
• W3167574390 hasConcept C185592680 @default.
• W3167574390 hasConcept C2775880066 @default.
• W3167574390 hasConcept C2776376580 @default.
• W3167574390 hasConcept C2776414213 @default.
• W3167574390 hasConcept C28859421 @default.
• W3167574390 hasConcept C55493867 @default.
• W3167574390 hasConcept C86803240 @default.
• W3167574390 hasConcept C95444343 @default.
• W3167574390 hasConceptScore W3167574390C104317684 @default.
• W3167574390 hasConceptScore W3167574390C119157956 @default.
• W3167574390 hasConceptScore W3167574390C11960822 @default.
• W3167574390 hasConceptScore W3167574390C14036430 @default.
• W3167574390 hasConceptScore W3167574390C173396325 @default.
• W3167574390 hasConceptScore W3167574390C181199279 @default.
• W3167574390 hasConceptScore W3167574390C185592680 @default.
• W3167574390 hasConceptScore W3167574390C2775880066 @default.
• W3167574390 hasConceptScore W3167574390C2776376580 @default.
• W3167574390 hasConceptScore W3167574390C2776414213 @default.
• W3167574390 hasConceptScore W3167574390C28859421 @default.
• W3167574390 hasConceptScore W3167574390C55493867 @default.
• W3167574390 hasConceptScore W3167574390C86803240 @default.
• W3167574390 hasConceptScore W3167574390C95444343 @default.
• W3167574390 hasIssue "S1" @default.
• W3167574390 hasLocation W31675743901 @default.
• W3167574390 hasOpenAccess W3167574390 @default.
• W3167574390 hasPrimaryLocation W31675743901 @default.
• W3167574390 hasRelatedWork W1895981298 @default.
• W3167574390 hasRelatedWork W1953044259 @default.
• W3167574390 hasRelatedWork W20337235 @default.
• W3167574390 hasRelatedWork W2051384458 @default.
• W3167574390 hasRelatedWork W2107901534 @default.
• W3167574390 hasRelatedWork W2109572947 @default.
• W3167574390 hasRelatedWork W2517899200 @default.
• W3167574390 hasRelatedWork W2771849436 @default.
• W3167574390 hasRelatedWork W2888018387 @default.
• W3167574390 hasRelatedWork W2739676309 @default.
• W3167574390 hasVolume "35" @default.
• W3167574390 isParatext "false" @default.
• W3167574390 isRetracted "false" @default.
• W3167574390 magId "3167574390" @default.
• W3167574390 workType "article" @default.