Research into the fatal neurodegenerative epilepsy called Lafora disease (LD) and biofuels research are surprisingly linked to a recently discovered family of enzymes called glucan phosphatases. Metabolism of starch in plants and glycogen in humans is dependent on the action of glucan phosphatases. EPM2A gene encodes laforin and recessive mutations in EPM2A result in LD. Laforin is a human glucan phosphatase and it removes phosphate from glycogen. In the absence of laforin activity, glycogen transforms into a hyper-phosphorylated, water-insoluble, starch-like Lafora body (LB). LBs are the suspected cause of neuronal apoptosis, neurodegeneration, and eventual death of LD patients. Similarly, in the absence of glucan phosphatases, plants cannot access the energy stored in starch and the starch granules grow in size while plant growth is stunted. We determined the x-ray crystal structure of multiple glucan phosphatases to gain insights into how this unique class of enzymes function. Defining molecular mechanisms of glucan phosphatases will advance our understanding of Lafora disease and glycogen metabolism.

Glucan phosphatases link Lafora progressive myoclonic epilepsy and biofuels research

246th National Meeting (2013)

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