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PXD027617

PXD027617 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleTargeted Protein Acetylation in Cells Using Heterobifunctional Molecules
DescriptionProtein acetylation is a central event in orchestrating diverse cellular processes. However, current strategies to investigate protein acetylation in cells are often non-specific 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 FKBP12F36V, 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-B subunit p65/RelA, and the tumor suppressor p53. We demonstrate that targeted acetylation with the AceTAG system is rapid, selective, reversible, and can be controlled in a dose-dependent fashion. AceTAG represents a useful strategy to modulate protein acetylation and will enable the exploration of targeted acetylation in basic biological and therapeutic contexts.
HostingRepositoryPRIDE
AnnounceDate2024-01-26
AnnouncementXMLSubmission_2024-01-26_07:05:52.707.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterLi Yun Chen
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListacetylated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Fusion Lumos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-07-28 02:30:27ID requested
12024-01-26 07:05:53announced
Publication List
Wang WW, Chen LY, Wozniak JM, Jadhav AM, Anderson H, Malone TE, Parker CG, Targeted Protein Acetylation in Cells Using Heterobifunctional Molecules. J Am Chem Soc, 143(40):16700-16708(2021) [pubmed]
10.1021/jacs.1c07850;
Keyword List
submitter keyword: targeted acetylation, acetylproteomics, p300/CBP, heterobifunctional molecules
Contact List
Christopher G. Parker
contact affiliationAssistant Professor, Department of Chemistry, The ScrippsResearch Institute
contact emailcparker@scripps.edu
lab head
Li Yun Chen
contact affiliationThe Scripps Research Institute
contact emaillichen@scripps.edu
dataset submitter
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Dataset FTP location
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