Acetylation, a post-translational modification, is increasingly recognized as a regulatory mechanism comparable to phosphorylation. This review explores the role of acetylation in regulating diverse cellular functions, including DNA recognition, protein stability, and protein-protein interactions. Acetylation is catalyzed by acetylases and reversed by deacetylases, with acetylases modifying a wide range of proteins, including transcription factors, nuclear import factors, and α-tubulin. The bromodomain, a conserved structure that recognizes acetylated residues, may serve as a signaling domain, similar to the SH2 domain in kinases. Acetylation of histones is known to enhance transcription, but its effects on non-histone proteins are also significant. For example, acetylation of transcription factors like p53 and E2F1 can either stimulate or inhibit DNA binding, depending on the site of modification. Acetylation also influences protein stability and nuclear import. The acetylation of histones may generate a recognition site for bromodomains, which are found in many proteins, including acetylases. Acetylases and deacetylases are regulated by various signaling pathways, including those involved in DNA repair and cell cycle progression. Phosphorylation can influence acetylation, as seen in the case of p53, where phosphorylation enhances acetylation. Similarly, hormone signaling can modulate acetylase activity, affecting nuclear receptor function and cell differentiation. While acetylation and phosphorylation share similarities in substrate diversity and regulatory functions, they differ in their mechanisms and signaling roles. Acetylation may not have a cascade-like signaling mechanism, unlike phosphorylation. However, both modifications can regulate key cellular processes in response to extracellular signals. Acetylation is still less well understood than phosphorylation, but its role in cellular regulation is becoming increasingly clear. The development of specific inhibitors for acetylases would be valuable for studying their in vivo functions. Overall, acetylation is emerging as a significant regulatory modification, comparable to phosphorylation in its biological relevance.Acetylation, a post-translational modification, is increasingly recognized as a regulatory mechanism comparable to phosphorylation. This review explores the role of acetylation in regulating diverse cellular functions, including DNA recognition, protein stability, and protein-protein interactions. Acetylation is catalyzed by acetylases and reversed by deacetylases, with acetylases modifying a wide range of proteins, including transcription factors, nuclear import factors, and α-tubulin. The bromodomain, a conserved structure that recognizes acetylated residues, may serve as a signaling domain, similar to the SH2 domain in kinases. Acetylation of histones is known to enhance transcription, but its effects on non-histone proteins are also significant. For example, acetylation of transcription factors like p53 and E2F1 can either stimulate or inhibit DNA binding, depending on the site of modification. Acetylation also influences protein stability and nuclear import. The acetylation of histones may generate a recognition site for bromodomains, which are found in many proteins, including acetylases. Acetylases and deacetylases are regulated by various signaling pathways, including those involved in DNA repair and cell cycle progression. Phosphorylation can influence acetylation, as seen in the case of p53, where phosphorylation enhances acetylation. Similarly, hormone signaling can modulate acetylase activity, affecting nuclear receptor function and cell differentiation. While acetylation and phosphorylation share similarities in substrate diversity and regulatory functions, they differ in their mechanisms and signaling roles. Acetylation may not have a cascade-like signaling mechanism, unlike phosphorylation. However, both modifications can regulate key cellular processes in response to extracellular signals. Acetylation is still less well understood than phosphorylation, but its role in cellular regulation is becoming increasingly clear. The development of specific inhibitors for acetylases would be valuable for studying their in vivo functions. Overall, acetylation is emerging as a significant regulatory modification, comparable to phosphorylation in its biological relevance.