PDLIM1 is a cytoskeletal adapter protein containing PDZ and LIM domains that assembles and organizes stress fibers through its interaction with α-actinin proteins. It regulates actin dynamics, focal adhesion formation, and cell polarity in fibroblasts, and coordinates cytoskeleton architecture during spermatid maturation through autophagy-mediated ectoplasmic specialization. In cancer biology, PDLIM1 acts as a tumor suppressor. In hepatocellular carcinoma (HCC), PDLIM1 suppresses metastasis by competitively binding α-actinin 4, preventing excessive F-actin accumulation and subsequent activation of Yes-associated protein signaling 1. Low PDLIM1 expression in metastatic HCC tissues predicts unfavorable prognosis. Conversely, in liver fibrosis, PDLIM1 is upregulated and promotes hepatic stellate cell activation and transdifferentiation into myofibroblasts, suggesting context-dependent roles 2. Recent studies identify PDLIM1 as a biomarker in age-related vascular disease. PDLIM1 expression is downregulated in atherosclerotic plaques and is associated with immune cell infiltration and macrophage differentiation patterns 3, 4. PDLIM1 also suppresses retinal neovascularization in diabetic retinopathy through β-catenin pathway inhibition, with increased levels conferring protection against pathological angiogenesis 5. No approved drugs targeting PDLIM1 have been identified in clinical trials, though its role as a modulator of Hippo and Wnt/β-catenin signaling suggests potential therapeutic relevance in cancer and vascular disease contexts.