Fig. 6: USP32 the function of many malignancies. | Cell Death Discovery

Fig. 6: USP32 the function of many malignancies.

From: USP32 deubiquitinase: cellular functions, regulatory mechanisms, and potential as a cancer therapy target

Fig. 6: USP32 the function of many malignancies.The alternative text for this image may have been generated using AI.

The expression of USP32 protein is negatively correlated with MicroRNAlet-7a in breast cancer, which can suppress USP32 expression and impede the growth of breast cancer cells. ETV1 controls the expression of USP32, which in turn stabilizes Rab35 by ubiquitinating Lys48 (K48) on Rab35 and increases exocrine secretion of imatinib-resistant gastrointestinal stromal tumors. USP32 supports the growth of acute myeloid leukemia (AML) through deubiquitinating and stabilizing Rap1b, while hsa_circ_0013880 controls USP32 expression in AML through miR-148a3p/miR-20a-5p. USP32 is extensively expressed in lung cancer tissues, where it dramatically speeds up cell division, encourages cell growth, and prevents cell death. USP32 contributes in the onset and progression of gastric cancer by controlling SHMT2, and USP32 enhances gastric carcinogenesis and cisplatin resistance in gastric cancer by eliminating ubiquitin and stabilizing SMAD2. USP32 increases resistance to YM155 in breast cancer cells through modulation of SLC35F2. By controlling the expression of FDFT1 protein, USP32 contributes to the development and progression of epithelial ovarian cancer. By controlling the cell cycle, DNA replication, basal excision repair, and mismatch repair in glioblastoma, USP32 promotes GBM.

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