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. Author manuscript; available in PMC: 2024 Oct 2.
Published in final edited form as: Mol Cancer Ther. 2024 Apr 2;23(4):478–491. doi: 10.1158/1535-7163.MCT-23-0312

Fig.6: QC6352 causes decreased KDM4A-C protein levels caused by ubiquitination.

Fig.6:

(A) QC6352 treatment of WiT49 and HEK293 causes reduction of KDM4A, B, and C on the protein level starting at six hours and persisting for at least 72 hours. This is accompanied by an increase in H3K36me3 and H3K9me3 (KDM4A-C targets). (B) The reduction in KDM4A, KDM4B, and KDM4C associated with QC6352 is abrogated by co-treatment with the proteasome inhibitor MG132. (C) Immunoprecipitation of ubiquitin followed by western blot for KDM4A, B, and C demonstrated a direct protein-protein interaction between KDM4A-C and ubiquitin in both untreated WiT49 and HEK293 cells. Equal amounts of protein from group were immunoprecipitated with ubiquitin antibody and the immunocomplexes were analyzed by western blot for KDM4A, KDM4B and KDM4C. Asterices indicate the relevant band and associated molecular weight for KDM4A, B, and C. (D) Immunoprecipitation of ubiquitin followed by western blot for KDM4A, B, and C demonstrated a direct protein-protein interaction between KDM4A, B, and C and ubiquitin that is increased in the presence of QC6352 treatment, and decreased by co-treatment with QC6352 and MG132 (proteasome inhibitor).