TALDO1 (transaldolase 1) catalyzes the rate-limiting step of the non-oxidative phase in the pentose phosphate pathway, converting sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into erythrose-4-phosphate and Ξ²-D-fructose 6-phosphate 1. Beyond its classical enzymatic function, TALDO1 exhibits moonlighting properties through subcellular localization between the nucleus and cytoplasm 2. When acetylated, TALDO1 translocates to the nucleus and interacts with BRCA1 to inhibit c-Myc transcriptional activation, thereby suppressing glycolytic enzyme expression independent of its enzymatic activity 2. HDAC6-mediated deacetylation at lysine 7 reduces TALDO1 protein stability and prevents its nuclear translocation, promoting tumor progression 2. TALDO1 is clinically significant across multiple diseases: it serves as a biomarker for breast cancer metastasis 3, shows altered expression in hepatocellular carcinoma where it's epigenetically regulated by p300/CBP 4, and is decreased in AMD-associated retinal pigmented epithelial cells, contributing to mitochondrial dysfunction through reduced NADPH availability 5. The gene maps to chromosome 11.4-p15.5 6, and its expression correlates with anti-VEGF therapy response in neovascular AMD 7.