{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang WW"],"funding":["NIAID NIH HHS","Scripps Research Institute","National Institutes of Health","NIH HHS"],"pagination":["16700-16708"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10793965"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["143(40)"],"pubmed_abstract":["Protein acetylation is a central event in orchestrating diverse cellular processes. However, current strategies to investigate protein acetylation in cells are often nonspecific or lack temporal and magnitude control. Here, we developed an acetylation tagging system, AceTAG, to induce acetylation of targeted proteins. The AceTAG system utilizes bifunctional molecules to direct the lysine acetyltransferase p300/CBP to proteins fused with the small protein tag FKBP12<sup>F36V</sup>, resulting in their induced acetylation. Using AceTAG, we induced targeted acetylation of a diverse array of proteins in cells, specifically histone H3.3, the NF-κB subunit p65/RelA, and the tumor suppressor p53. We demonstrate that targeted acetylation with the AceTAG system is rapid, selective, reversible and ca"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Targeted Protein Acetylation in Cells Using Heterobifunctional Molecules."],"pmcid":["PMC10793965"],"funding_grant_id":["S10 OD021550","T32 AI007244"],"pubmed_authors":["Jadhav AM","Chen LY","Parker CG","Wang WW","Malone TE","Wozniak JM","Anderson H"],"additional_accession":[]},"is_claimable":false,"name":"Targeted Protein Acetylation in Cells Using Heterobifunctional Molecules.","description":"Protein acetylation is a central event in orchestrating diverse cellular processes. However, current strategies to investigate protein acetylation in cells are often nonspecific or lack temporal and magnitude control. Here, we developed an acetylation tagging system, AceTAG, to induce acetylation of targeted proteins. The AceTAG system utilizes bifunctional molecules to direct the lysine acetyltransferase p300/CBP to proteins fused with the small protein tag FKBP12<sup>F36V</sup>, resulting in their induced acetylation. Using AceTAG, we induced targeted acetylation of a diverse array of proteins in cells, specifically histone H3.3, the NF-κB subunit p65/RelA, and the tumor suppressor p53. We demonstrate that targeted acetylation with the AceTAG system is rapid, selective, reversible and ca","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Oct","modification":"2026-05-29T10:05:00.177Z","creation":"2025-04-05T12:40:49.091Z"},"accession":"S-EPMC10793965","cross_references":{"pubmed":["34592107"],"doi":["10.1021/jacs.1c07850"]}}