EPM2A encodes laforin, a glucan phosphatase that regulates glycogen metabolism and structure. Laforin functions as part of a protein complex with malin to control glycogen synthesis and prevent accumulation of abnormal glycogen 1. The enzyme dephosphorylates glycogen, maintaining proper glucose polymer architecture and preventing the formation of toxic polyglucosans 2. Laforin also negatively regulates mTOR signaling and promotes macroautophagy, contributing to protein quality control via the ubiquitin-proteasome system 3. EPM2A mutations cause Lafora disease, an autosomal recessive progressive myoclonus epilepsy characterized by accumulation of abnormal glycogen structures called Lafora bodies in the brain, liver, muscle, and sweat glands 2. Disease onset typically occurs in early adolescence with seizures, followed by progressive neurological decline including cognitive deterioration and ataxia 4. The condition is invariably fatal, with death occurring within 10 years of symptom onset 2. Clinical significance is limited by poor responsiveness to antiepileptic drugs. However, recent gene therapy approaches using adeno-associated viral delivery of human EPM2A ameliorated neurological symptoms, reduced epileptic activity, and decreased Lafora body formation in mouse models, representing promising therapeutic potential 1. Therapeutic strategies targeting reduced brain glycogen synthesis appear particularly promising 2.