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. Author manuscript; available in PMC: 2021 Jan 18.
Published in final edited form as: Cancer Res. 2019 Nov 18;80(3):430–443. doi: 10.1158/0008-5472.CAN-19-1033

Figure 4. The USP22-sensitive ubiquitylome reveals altered modification of DNA repair-related proteins.

Figure 4.

(A) Ubiscan workflow and models used for analyses. LNCaP parental cells were transfected with shUSP22 or USP22. Three samples (LNCaP: parental, shUSP22, and USP22) were run as duplicate injections for a total of 6 LC-MS/MS experiments. (B) Differential ubiquitylation of histones H2A and H2B upon USP22 knockdown and overexpression compared to LNCaP parental control. (C) Ubiscan analysis demonstrates differentially ubiquitylated peptides upon USP22 overexpression and USP22 knockdown. Putative targets of USP22 differential ubiquitination designated as >1.5-fold decreased peptide ubiquitylation in LN-USP22 compared to control and >1.5-fold increased peptide ubiquitylation in LN-shUSP22 compared to parental control (Peptides denoted in purple). (D) Putative direct targets of USP22 function as determined by (C) with DNA repair-related peptides designated by inclusion in gene set enrichment analysis pathways (KEGG or Hallmark GSEA).