Publications by authors named "Punitee Garyali"
Article Synopsis
- Lafora disease is a progressive form of myoclonus epilepsy caused by mutations in the EPM2A or EPM2B genes, which lead to abnormal glycogen accumulation in various organs, including the brain and muscles.
- Research on mouse models lacking these genes showed decreased autophagy and proteasomal activity linked to disrupted protein degradation pathways, although their response to ER stress remained unaffected.
- The findings suggest that both laforin and malin mutations affect cellular quality control processes, possibly due to the overaccumulation of glycogen, with evidence indicating that malin has a role that is independent of laforin in lysosomal function.
Lafora disease (LD), a progressive form of inherited epilepsy, is associated with widespread neurodegeneration and the formation of polyglucosan bodies in the neurons. Laforin, a protein phosphatase, and malin, an E3 ubiquitin ligase, are two of the proteins that are defective in LD. We have shown recently that laforin and malin (referred together as LD proteins) are recruited to aggresome upon proteasomal blockade, possibly to clear misfolded proteins through the ubiquitin-proteasome system (UPS).
View Article and Find Full Text PDF