Abstract
Tau is a cytoskeletal protein whose malfunction has been linked to the development of multiple neurodegenerative diseases in the brain. Tau’s main function in the brain is to act as a regulator protein for stabilizing and maintaining microtubules inside axons. Tau is mainly localized in the distal portion of the axon and guides tubulin to form microtubule networks. A variety of kinases are known to phosphorylate Tau and suppress its function. Hyperphosphorylation of Tau by these kinases has been linked to tau malfunction, dissociation from microtubules, and aggregation in neurons. This aggregation around neurons inhibits intraneuronal communication and results in neuron death and degeneration of brain tissue. This malfunction of Tau is associated with a group of neurodegenerative diseases called Tauopathies. Major Tauopathies include Alzheimer’s disease, frontotemporal dementia with parkinsonism, progressive supranuclear palsy (PSP), corticobasal degeneration (CBD), and Pick’s disease (PiD). Lgl or lethal giant larvae is a tumor suppressor gene in Drosophila Melanogaster with multiple human homologs, which encode a cytoskeletal protein “required for the change in shape and polarity acquisition of epithelial cells, and also for asymmetric division of neuroblasts”1 . One of lgl’s main functions is to establish apical-basal cell polarity and regulate cell proliferation. When this gene is mutated in flies, they demonstrate “a gradual loss of tissue architecture and an extended larval life in which cell proliferation never ceases and no differentiation occurs, resulting in pre pupal lethality”2 . A similar study was performed by a previous student that discovered that flies that lacked one copy of the lgl gene (lgl[-]/+) had significantly higher Tau toxicity levels than the controls. This likely indicates that lgl plays a role in suppressing Tau toxicity and down regulating its phosphorylation.