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Title:
Functions and mechanisms of non-histone protein acetylation | Nature Reviews Molecular Cell Biology
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Nε-lysine acetylation was discovered more than half a century ago as a post-translational modification of histones and has been extensively studied in the context of transcription regulation. In the past decade, proteomic analyses have revealed that non-histone proteins are frequently acetylated and constitute a major portion of the acetylome in mammalian cells. Indeed, non-histone protein acetylation is involved in key cellular processes relevant to physiology and disease, such as gene transcription, DNA damage repair, cell division, signal transduction, protein folding, autophagy and metabolism. Acetylation affects protein functions through diverse mechanisms, including by regulating protein stability, enzymatic activity, subcellular localization and crosstalk with other post-translational modifications and by controlling protein–protein and protein–DNA interactions. In this Review, we discuss recent progress in our understanding of the scope, functional diversity and mechanisms of non-histone protein acetylation. Non-histone-lysine acetylation affects protein functions by modulating protein stability, interactions, subcellular localization and enzymatic activity and through crosstalk with other post-translational modifications. Acetylation regulates many cellular processes, such as transcription, DNA repair, signal transduction, protein folding and autophagy.
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nature portfolio journals permissions reprints privacy policy nature portfolio author information authors protein post-translational modifications additional information publisher advertising n-terminal acetyltransferase naa10/ard1 cbp/p300-mediated h3k18/27ac post-translational modifications european research council social media protein research dysregulated acetyl/sumo switch targets lineage-specific tumours development nucleotide excision repair synthesis ubiquitin-selective quality-control autophagy post-translational modification /irs-2/ras/erk1/2 signaling p300/cbp-mediated p53 acetylation acetylation-induced tdp-43 pathology horizon 2020 research gcn5/pcaf-mediated h3k9ac interferon-inducible protein ifi16 site-specific dna binding author correction author correspondence stress-inducible sumo modification nuclear acetyl-coa production pcaf/gcn5-mediated acetylation sirt1-mediated enampt secretion aspirin-mediated lysine acetylome acetyltransferases creb-binding protein enhance lysine n-acetylation ε-amino side chain p53 c-terminal domain acetylation/deacetylation-sumoylation switch hsf1-dependent chaperone program lysine acetyl-transferase gene mass spectrometry-based proteomics report proteome-wide surveys fatty acid oxidation sirtuin1-regulated lysine acetylation exome-sequencing identifies mutations human cml-bc cells nad-dependent deacetylase sirt1 enzyme-independent nepsilon-acetylation phosphorylation-dependent sumo modification
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