NHLRC1 encodes malin, an E3 ubiquitin ligase that plays a critical role in preventing abnormal glycogen accumulation and protein aggregation. The protein functions in partnership with the phosphatase EPM2A/laforin to regulate glycogen metabolism through multiple degradation pathways 1. NHLRC1 promotes ubiquitin-dependent degradation of glycogen-targeting protein phosphatase subunits and other substrates via the ubiquitin-proteasome system, while also facilitating proteasome-independent degradation through macroautophagy 1. Mutations in NHLRC1 cause Lafora disease, a fatal autosomal recessive progressive myoclonus epilepsy characterized by teenage onset and accumulation of polyglucosan bodies 23. The disease manifests with myoclonus, tonic-clonic seizures, visual hallucinations, and progressive neurological deterioration typically beginning at 12-15 years of age 3. Nearly 100 distinct mutations have been identified in NHLRC1, with missense mutations comprising nearly half of all variants 3. Mutant forms of malin show altered subcellular localization, which may contribute to disease pathogenesis 4. Complete gene deletions have been associated with particularly severe phenotypes 5.