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Lysine Acetylation (lysine + acetylation)
Selected AbstractsLysine Acetylation: The Tale of a Modification from Transcription Regulation to MetabolismCHEMBIOCHEM, Issue 11 2010Mohammed Arif Dr. Reversible lysine acetylation is an important modification involved in the regulation of gene expression. Acetyl-CoA and NAD+ are major determinants of this modification, NAD+ levels being regulated by the cellular redox status. Recent reports have shown that lysine acetylation also regulates metabolic processes, thus linking the central metabolic process to gene expression. [source] Histone deacetylases as transducers and targets of nuclear signalingJOURNAL OF CELLULAR BIOCHEMISTRY, Issue 5 2008Donald R. Walkinshaw Abstract Histone deacetylase (HDAC) activity was first discovered about 40 years ago, but it was not until the molecular identification of the first HDACs in 1996 that this family of enzymes gained prominence. In addition to histones, HDACs reverse lysine acetylation of various non-histone proteins located in the nucleus and the cytoplasm. Here, we examine the nuclear roles of these enzymes, with a specific focus on their active crosstalk with different chromatin regulators. J. Cell. Biochem. 104: 1541,1552, 2008. © 2008 Wiley-Liss, Inc. [source] Calorie restriction alters mitochondrial protein acetylationAGING CELL, Issue 5 2009Bjoern Schwer Summary Calorie restriction (CR) increases lifespan in organisms ranging from budding yeast through mammals. Mitochondrial adaptation represents a key component of the response to CR. Molecular mechanisms underlying this adaptation are largely unknown. Here we show that lysine acetylation of mitochondrial proteins is altered during CR in a tissue-specific fashion. Via large-scale mass spectrometry screening, we identify 72 candidate proteins involved in a variety of metabolic pathways with altered acetylation during CR. Mitochondrial acetylation changes may play an important role in the pro-longevity CR response. [source] c-Jun Expression, activation and function in neural cell death, inflammation and repairJOURNAL OF NEUROCHEMISTRY, Issue 4 2008Gennadij Raivich Abstract Up-regulation of c-Jun is a common event in the developing, adult as well as in injured nervous system that serves as a model of transcriptional control of brain function. Functional studies employing in vivo strategies using gene deletion, targeted expression of dominant negative isoforms and pharmacological inhibitors all suggest a three pronged role of c-Jun action, exercising control over neural cell death and degeneration, in gliosis and inflammation as well as in plasticity and repair. In vitro, structural and molecular studies reveal several non-overlapping activation cascades via N-terminal c-Jun phosphorylation at serine 63 and 73 (Ser63, Ser73), and threonine 91 and 93 (Thr91, Thr93) residues, the dephosphorylation at Thr239, the p300-mediated lysine acetylation of the near C-terminal region (Lys268, Lys271, Lys 273), as well as the Jun-independent activities of the Jun N-terminal family of serine/threonine kinases, that regulate the different and disparate cellular responses. A better understanding of these non-overlapping roles in vivo could considerably increase the potential of pharmacological agents to improve neurological outcome following trauma, neonatal encephalopathy and stroke, as well as in neurodegenerative disease. [source] Lysine Acetylation: The Tale of a Modification from Transcription Regulation to MetabolismCHEMBIOCHEM, Issue 11 2010Mohammed Arif Dr. Reversible lysine acetylation is an important modification involved in the regulation of gene expression. Acetyl-CoA and NAD+ are major determinants of this modification, NAD+ levels being regulated by the cellular redox status. Recent reports have shown that lysine acetylation also regulates metabolic processes, thus linking the central metabolic process to gene expression. [source] | ||||||||||