Cysteine S-acetylation is a widespread post-translational modification on metabolic proteins [PDF]
Protein acetylation is a fundamental regulatory mechanism occurring primarily on lysine amino acids. Here we report systematic in vivo characterization of cysteine S-acetylation as a widespread post-translational modification in mammalian tissues.
E. Keith Keenan +4 more
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Non-enzymatic N-acetylation of Lysine Residues by AcetylCoA Often Occurs via a Proximal S-acetylated Thiol Intermediate Sensitive to Glyoxalase II [PDF]
Summary: Acetyl coenzyme A (AcCoA), a key intermediate in mitochondrial metabolism, N-acetylates lysine residues, disrupting and, in some cases, regulating protein function.
Andrew M. James +6 more
doaj +2 more sources
Skeletal muscle alpha actin acetylation enhances myosin binding and increases calcium sensitivity [PDF]
Skeletal muscle alpha actin (ACTA1) is important for muscle contraction and relaxation, with historical studies focused on ACTA1 mutations in muscle dysfunction.
Samantha S. Romanick +7 more
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KAT6A acetyltransferase accelerates colorectal cancer progression through upregulating BRD1 protein expression via acetylation modification. [PDF]
Liang Y, Shen Y, Liang S, Wu S, Feng X.
europepmc +2 more sources
Contribution of Nε-lysine Acetylation towards Regulation of Bacterial Pathogenesis
Nε-lysine acetylation is an important, dynamic regulatory posttranslational modification (PTM) that is common in bacteria. Protein acetylomes have been characterized for more than 30 different species, and it is known that acetylation plays important ...
Jackson Luu, Valerie J. Carabetta
doaj +1 more source
Api5, is a known anti-apoptotic and nuclear protein that is responsible for inhibiting cell death in serum-starved conditions. The only known post-translational modification of Api5 is acetylation at lysine 251 (K251).
Virender Kumar Sharma, Mayurika Lahiri
doaj +1 more source
BackgroundLysine acetylation and deacetylation are posttranslational modifications that are able to link extracellular signals to intracellular responses. However, knowledge regarding the status of lysine regulators in urological cancers is still unknown.
Jian Zhang +4 more
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Acetylation-mediated suppression of transcription-independent memory: bidirectional modulation of memory by acetylation. [PDF]
Learning induced changes in protein acetylation, mediated by histone acetyl transferases (HATs), and the antagonistic histone deacetylases (HDACs) play a critical role in memory formation. The status of histone acetylation affects the interaction between
Katja Merschbaecher +2 more
doaj +1 more source
Position-specific analysis and prediction for protein lysine acetylation based on multiple features. [PDF]
Protein lysine acetylation is a type of reversible post-translational modification that plays a vital role in many cellular processes, such as transcriptional regulation, apoptosis and cytokine signaling.
Sheng-Bao Suo +6 more
doaj +1 more source
Acetylation-dependent coupling between G6PD activity and apoptotic signaling
Lysine acetylation has been discovered in thousands of non-histone human proteins, including most metabolic enzymes. Deciphering the functions of acetylation is key to understanding how metabolic cues mediate metabolic enzyme regulation and cellular ...
Fang Wu +7 more
doaj +1 more source

