Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions

@article{Choudhary2009LysineAT,
  title={Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions},
  author={Chunaram Choudhary and Chanchal Kumar and Florian Gnad and Michael L. Nielsen and Michael Rehman and Tobias C. Walther and Jesper V. Olsen and Matthias Mann},
  journal={Science},
  year={2009},
  volume={325},
  pages={834 - 840}
}
Lysine Acetylation Catalog Covalent posttranslational modification is an essential cellular regulatory mechanism by which the activity of proteins can be controlled. Advances in mass spectrometry made it possible for Choudhary et al. (p. 834, published online 16 July) to assess the prevalence of lysine acetylation throughout the whole proteome. Acetylation is much more widespread than previously appreciated and occurs on proteins participating in all sorts of biological functions. Acetylation… 
Ancient Regulatory Role of Lysine Acetylation in Central Metabolism
TLDR
A proteomic analysis of 48 phylogenetically distant bacteria discovered conserved acetylation sites on catalytically essential lysine residues that are invariant throughout evolution, suggesting that acetylations may play a direct role in metabolic regulation by switching off enzyme activity.
Protein acetylation and deacetylation: An important regulatory modification in gene transcription (Review)
TLDR
The discovery of specific protein acetylation sites using bioinformatic tools can greatly aid the understanding of the underlying mechanisms of protein acetolation involved in related physiological and pathological processes.
Lysine Acetylation of Proteins and Its Characterization in Human Systems.
TLDR
This article summarizes some established biochemical information about how protein acetylation takes place and is regulated, in order to lay the foundation for subsequent descriptions of strategies used by the lab and others either to directly study acetylated proteins of an individual factor or to identify groups of proteins targeted for acetylations that can then be examined in isolation.
The biology of lysine acetylation integrates transcriptional programming and metabolism
TLDR
A focus of this work is to present the widespread and dynamic nature of lysine acetylation and highlight the nexus that exists between epigenetic-directed transcriptional regulation and metabolism.
Comprehensive profiling of protein lysine acetylation in Escherichia coli.
TLDR
This study has demonstrated that the combined approach is powerful for identification and characterization of protein lysine acetylation on a large scale and provides a series of important information including localization, networks and characterize of acetylome.
Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation
Lysine acetylation is a reversible posttranslational modification that occurs at thousands of sites on human proteins. However, the stoichiometry of acetylation remains poorly characterized, and is
Lysine Acetylation Stoichiometry Analysis at the Proteome Level.
TLDR
A method to identify lysine acetylation sites and estimate their site occupancy at the proteome scale is described, which relies on a high-resolution mass spectrometry-based proteomics approach, which includes a specific chemical acetylations reaction on unmodified lysines residues that carry heavy isotopes.
Protein lysine acetylation and its role in different human pathologies: a proteomic approach
TLDR
This review presents an overview of the main participant elements, the scenario in the development of protein lysine acetylation, and its role in different human pathologies, and some intermediate mediators in the acetylations process have been projected as therapeutic targets.
Mitochondria Lysine Acetylation and Phenotypic Control.
  • F. Ciregia
  • Biology, Chemistry
    Advances in experimental medicine and biology
  • 2019
TLDR
Modifications in lysine acetylation status can directly alter mitochondrial function and be linked to human diseases such as metabolic diseases, cancer, myocardial injury and neurodegenerative diseases.
...
...

References

SHOWING 1-10 OF 71 REFERENCES
Acetylation: a regulatory modification to rival phosphorylation?
TLDR
This review sets out what the authors know about the broader substrate specificity and regulation of acetylases and goes on to compare acetylation with the process of phosphorylation.
Functions of site-specific histone acetylation and deacetylation.
Histone acetylation regulates many cellular processes, and specific acetylation marks, either singly or in combination, produce distinct outcomes. For example, the acetylation pattern on newly
Lysine acetylation and the bromodomain: a new partnership for signaling
  • Xiang-Jiao Yang
  • Biology, Chemistry
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 2004
TLDR
The relationship between acetyllysine and bromodomains is reminiscent of the specific recognition of phosphorylated residues by phospho‐specific binding modules such as SH2 domains and 14‐3‐3 proteins.
The Double-Histone-Acetyltransferase Complex ATAC Is Essential for Mammalian Development
TLDR
By targeted disruption of the Atac2 locus in mice, this work demonstrates for the first time the essential role of the ATAC complex in mammalian development, histone acetylation, cell cycle progression, and prevention of apoptosis during embryogenesis.
Acetylation of Conserved Lysines in the Catalytic Core of Cyclin-Dependent Kinase 9 Inhibits Kinase Activity and Regulates Transcription
TLDR
It is shown that cellular GCN5 and P/CAF, members of theGCN5-related N-acetyltransferase family of histone acetyltransferases, regulate CDK9 function by specifically acetylating the catalytic core of the enzyme and, in particular, a lysine that is essential for ATP coordination and the phosphotransfer reaction.
...
...