{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPSMD10, also known as gankyrin or p28, is an evolutionarily conserved non‐ATPase subunit of the 26S proteasome that is composed of multiple ankyrin repeats forming an extended, curved scaffold. Its unique structure enables extensive protein–protein interactions with key cell cycle regulators such as cyclin‐dependent kinase 4, the retinoblastoma protein (Rb) and the E3 ubiquitin ligase MDM2. Through these interactions, PSMD10 facilitates the degradation of tumor suppressors (e.g. p53 and Rb) and modulates NF‐κB signaling, thereby linking proteasome assembly with cell cycle control and survival pathways."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOverexpression of PSMD10 has been observed in a wide range of malignancies—including hepatocellular carcinoma, colorectal, pancreatic, ovarian, esophageal, breast, cervical, thyroid and gastric cancers—where it exerts potent oncogenic functions. By accelerating the proteasomal degradation of tumor suppressors and by modulating key signaling cascades such as PI3K–AKT, β‐catenin/c‐Myc, STAT3 and NF‐κB, PSMD10 promotes epithelial–mesenchymal transition, autophagy, metabolic reprogramming, cell proliferation, invasion, metastasis and chemoresistance. These multifaceted roles contribute to aggressive tumor behavior and poor clinical prognoses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "46"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecent studies also reveal that PSMD10 is intricately regulated at the post‐transcriptional and signaling levels. MicroRNAs (for example, miR‑214 and miR‑605) have been shown to directly target PSMD10 mRNA to restore p53 function and modulate cell cycle progression. In parallel, feedback loops with pathways involved in oxidative stress (via Nrf2/Keap1) and inflammation (via interleukin and IRAK1 signaling) further adjust its expression and activity. 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