Journal
CHEMICAL REVIEWS
Volume 118, Issue 3, Pages 340-376Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.chemrev.7b00181
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Funding
- UCSF Discovery Fellows Program
- American Society for Microbiology Robert D. Watkins Fellowship
- AmfAR Institute for HIV Cure Research
- NIH [R01AI083139-06, R01DA043142, 1DP1DA038043, 5R24 DK085610-06, R21AG051111]
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Post-translational acetylation of lysine residues has emerged as a key regulatory mechanism in all eukaryotic organisms. Originally discovered in 1963 as a unique modification of histones, acetylation marks are now found on thousands of nonhistone proteins located in virtually every cellular compartment. Here we summarize key findings in the field of protein acetylation over the past 20 years with a focus on recent discoveries in nuclear, cytoplasmic, and mitochondrial compartments. Collectively, these findings have elevated protein acetylation as a major post-translational modification, underscoring its physiological relevance in gene regulation, cell signaling, metabolism, and disease.
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