Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 34, Issue 11, Pages 571-578Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2009.06.010
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Funding
- NCI NIH HHS [R01 CA090465, R01 CA090465-08, R01 CA098172-06, R01 CA098172] Funding Source: Medline
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Protein phosphorylation is regulated dynamically in eukaryotic cells via modulation of the enzymatic activity of kinases and phosphatases. Like phosphorylation, acetylation has emerged as a critical regulatory protein modification that is altered dynamically in response to diverse cellular cues. Moreover, acetyltransferases and deacetylases are tightly linked to cellular signaling pathways. Recent studies provide clues about the mechanisms utilized to regulate acetyltransferases and deacetylases. The therapeutic value of deacetylase inhibitors suggests that understanding acetylation pathways will directly impact our ability to rationally target these enzymes in patients. Recently discovered mechanisms that directly regulate the catalytic activity of acetyltransferases and deacetylases provide exciting new insights about these enzymes.
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