Fig. 5: VCP recruits USP2 through deubiquitylation modification to maintain FASN stability. | Cell Death & Disease

Fig. 5: VCP recruits USP2 through deubiquitylation modification to maintain FASN stability.

From: VCP enhances autophagy-related osteosarcoma progression by recruiting USP2 to inhibit ubiquitination and degradation of FASN

Fig. 5

A Venn diagram showing 14 candidate proteins obtained, by overlapping VCP-IP/MS, and deubiquitination-associated proteins from web databases. B OS cells lysates were immunoprecipitated with FASN, VCP and USP2 antibodies, respectively, to detect endogenous protein interactions. C 293 T cell lysates were transfected with HA-tagged FASN, FLAG-tagged USP2 and MYC-tagged VCP plasmids, immunoprecipitated with tagged antibodies, respectively, followed by immunoblotting to detect exogenous protein interactions. D Representative images (left) and the quantification (right) of immunofluorescence demonstrate the localization of USP2 and VCP proteins in 143B and U2OS cells. E Diagram of VCP and USP2 molecular docking patterns. F USP2 truncated structure. The full- length VCP, consisting of 605 amino acids, is divided into four structural domains: 1-403,200-605,200-403 and Δ200-403. G 293 T cells were transfected with MYC-labeled full-length VCP and FLAG-labeled full-length USP2 and its truncated structure region. Cell lysates were immunoprecipitated with anti-FLAG antibody or anti-MYC antibody, respectively. Western blot assay was conducted to identify the expression of the MYC probe and FLAG. H Total levels of FASN ubiquitinated proteins in OS cells were detected by Western blot, transfected with Ca-VCP, Ci-USP2 or co-transfected.

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