ZFPL1 (zinc finger protein-like 1) is a multifunctional protein with both structural and regulatory roles in cancer biology. At the cellular level, ZFPL1 is a conserved integral membrane protein required for cis-Golgi integrity and efficient ER-to-Golgi transport through direct interaction with the cis-Golgi matrix protein GM130 1. ZFPL1 contains zinc finger domains and a likely ring domain at its N-terminus, suggesting DNA-binding and possible E3 ubiquitin ligase activity 2. In cancer pathology, ZFPL1 emerges as a key oncogenic driver across multiple malignancies. In prostate cancer, ZFPL1 is upregulated by calcitonin and androgens, exhibits neuroendocrine localization, and serum levels are 4-fold higher in cancer patients than controls, establishing it as a non-invasive biomarker 3. ZFPL1 knockdown decreases prostate cancer cell proliferation and invasion via PI3K-Akt pathway inhibition 3. In colorectal cancer, ZFPL1 stabilizes argininosuccinate synthase 1 (ASS1) to activate urea cycle metabolism and promotes M2 macrophage-mediated immunosuppression; Salvianolic acid B inhibits ZFPL1-ASS1 binding and synergizes with anti-PD-1 therapy 4. In gastric cancer, ZFPL1 knockdown induces autophagy-dependent cell death through GM130 interaction 5. In lung cancer, elevated serum ZFPL1 shows diagnostic accuracy (AUC 0.921) and monitoring potential for treatment response 6.