KBTBD7 functions as a substrate adapter protein within the CUL3-RING ubiquitin ligase complex, mediating K48-linked ubiquitination and proteasomal degradation of multiple target proteins 1. The protein's primary mechanism involves its BTB domain and kelch repeats, which facilitate substrate recognition and transcriptional activation 2. KBTBD7 controls RAC1 signaling by targeting the guanine exchange factor TIAM1 for degradation, thereby regulating cytoskeleton organization, cell migration, and proliferation 1. This ubiquitination process requires cooperation with GABARAP proteins for membrane-restricted activity 1. KBTBD7 demonstrates significant disease relevance across multiple pathologies. In pituitary adenomas, it regulates dopamine receptor DRD2 degradation, with high KBTBD7 expression correlating with dopamine agonist resistance 3. In non-small cell lung cancer, KBTBD7 promotes tumor progression by enhancing PTEN degradation and activating EGFR/PI3K/AKT signaling 4. Additionally, KBTBD7 contributes to septic lung injury by promoting ferroptosis and mitochondrial dysfunction 5. The protein also participates in inflammatory responses, as its knockdown reduces inflammation in dental pulp fibroblasts through the miR-21/KBTBD7 axis and NF-κB pathway modulation 6. These findings establish KBTBD7 as a potential therapeutic target across multiple disease contexts.