The article reviews the recent advancements in understanding histone acetylation and its broader implications beyond histones. It highlights the identification of acetylases and deacetylases, which have been found to modify a wide range of proteins, including transcription factors, nuclear import factors, and α-tubulin. The review discusses the regulatory mechanisms of acetylation, such as the involvement of kinases and hormonal signals, and compares acetylation with phosphorylation in terms of substrate specificity, function, and signaling. Despite some similarities, the article notes differences, such as the lack of an acetylation cascade and the lower prevalence of acetylases compared to kinases. The conclusion emphasizes the potential of acetylation as a significant regulatory modification, comparable to phosphorylation, and calls for further research to fully understand its role in cellular processes.The article reviews the recent advancements in understanding histone acetylation and its broader implications beyond histones. It highlights the identification of acetylases and deacetylases, which have been found to modify a wide range of proteins, including transcription factors, nuclear import factors, and α-tubulin. The review discusses the regulatory mechanisms of acetylation, such as the involvement of kinases and hormonal signals, and compares acetylation with phosphorylation in terms of substrate specificity, function, and signaling. Despite some similarities, the article notes differences, such as the lack of an acetylation cascade and the lower prevalence of acetylases compared to kinases. The conclusion emphasizes the potential of acetylation as a significant regulatory modification, comparable to phosphorylation, and calls for further research to fully understand its role in cellular processes.