Proteomics

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Identification of the E3 ligase(s) recruited by 955 to degrade CDK9

ABSTRACT: PROTACs induce the degradation of target proteins by hijacking an E3 ligase. However, it is usually difficult to directly identify the E3 ligase recruited by a new E3 ligase ligand in a PROTAC using the co-immunoprecipitation method because the formation of the complex is transient and very dynamic. TurboID assay is a powerful proximity labeling method that can sensitively detect weak and transient protein-protein interactions by biotinylating proteins that interact with a bait protein fused with an engineered biotin ligase. Here, we adapted TurboID technology to identify and characterize the specific E3 ligase(s) recruited by 955, a potent piperlongumine (PL)-SNS-032 conjugated CDK9 PROTAC, to mediate CDK9 degradation.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

DISEASE(S): Disease Free

SUBMITTER: Dongwen Lyu  

LAB HEAD: Dongwen Lv

PROVIDER: PXD039401 | Pride | 2024-05-24

REPOSITORIES: Pride

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Publications

Proteolysis targeting chimeras (PROTACs) are bifunctional molecules that degrade target proteins through recruiting E3 ligases. However, their application is limited in part because few E3 ligases can be recruited by known E3 ligase ligands. In this study, we identified piperlongumine (PL), a natural product, as a covalent E3 ligase recruiter, which induces CDK9 degradation when it is conjugated with SNS-032, a CDK9 inhibitor. The lead conjugate 955 can potently degrade CDK9 in a ubiquitin-prote  ...[more]

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