Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease [PDF]
Current Opinion in Chemical Biology, 2018 Lipoylation is a rare, but highly conserved lysine posttranslational modification. To date, it is known to occur on only four multimeric metabolic enzymes in mammals, yet these proteins are staples in the core metabolic landscape.
Ileana Cristea
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FDX1 regulates cellular protein lipoylation through direct binding to LIAS [PDF]
Journal of Biological Chemistry, 2023 Abstract Ferredoxins are a family of iron-sulfur (Fe-S) cluster proteins that serve as essential electron donors in numerous cellular processes that are conserved through evolution. The promiscuous nature of ferredoxins as electron donors enables them to participate in many metabolic processes including steroid, heme, vitamin D and Fe-S
Squire Booker +2 more
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Boosting energy metabolism and biosynthesis in diverse organisms by a common bacterial salvage lipoylation protein [PDF]
Nature CommunicationsLipoylation is a highly conserved post-translational modification (PTM) crucial for energy metabolism enzymes, with distinct pathways across organisms. Whereas bacteria like Escherichia coli inherit both salvage and de novo pathways, only the latter is ...
Runqing Yang +7 more
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Glycine decarboxylase maintains mitochondrial protein lipoylation to support tumor growth [PDF]
Cell Metabolism, 2022 The folic acid cycle mediates the transfer of one-carbon (1C) units to support nucleotide biosynthesis. While the importance of serine as a mitochondrial and cytosolic donor of folate-mediated 1C units in cancer cells has been thoroughly investigated, a potential role of glycine oxidation remains unclear.
Boris Sarvin +2 more
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Genetic dissection of the mitochondrial lipoylation pathway in yeast [PDF]
BMC Biology, 2021 Background Lipoylation of 2-ketoacid dehydrogenases is essential for mitochondrial function in eukaryotes. While the basic principles of the lipoylation processes have been worked out, we still lack a thorough understanding of the details of this ...
Laura P. Pietikäinen +4 more
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Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum. [PDF]
PLoS Pathogens, 2007 Lipoic acid (LA) is an essential cofactor of alpha-keto acid dehydrogenase complexes (KADHs) and the glycine cleavage system. In Plasmodium, LA is attached to the KADHs by organelle-specific lipoylation pathways.
Svenja Günther +8 more
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Mitochondrial Protein Lipoylation and the 2-Oxoglutarate Dehydrogenase Complex Controls HIF1α Stability in Aerobic Conditions [PDF]
Cell Metabolism, 2016 Hypoxia-inducible transcription factors (HIFs) control adaptation to low oxygen environments by activating genes involved in metabolism, angiogenesis, and redox homeostasis. The finding that HIFs are also regulated by small molecule metabolites highlights the need to understand the complexity of their cellular regulation.
Stephen P Burr +2 more
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LipoFNT: Lipoylation Sites Identification with Flexible Neural Tree
Complexity, 2019 Lysine lipoylation is a special type of posttranslational modification in both prokaryotes’ and eukaryotes’ proteomics researches. Such a modification takes part in several significant biological processions and plays a key role in the cellular level. In
Wenzheng Bao +3 more
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The amidase domain of lipoamidase specifically inactivates lipoylated proteins in vivo.
PLoS ONE, 2009 BackgroundIn the 1950s, Reed and coworkers discovered an enzyme activity in Streptococcus faecalis (Enterococcus faecalis) extracts that inactivated the Escherichia. coli and E.
Maroya D Spalding, Sean T Prigge
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Silencing SLC31A1 attenuates high glucose plus copper-induced cuproptosis-like signaling, oxidative stress, and barrier dysfunction in human retinal microvascular endothelial cells [PDF]
International Journal of OphthalmologyAIM: To examine whether SLC31A1 knockdown protects human retinal microvascular endothelial cells (HRMECs) exposed to high glucose and copper. METHODS: HRMECs were exposed to normal glucose (5 mmol/L) or high glucose (30 mmol/L), with or without 50 μmol/L
Ying Li, Meng Chen, Han-Guang Dong
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