Authors:

Satvik Paduri

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About Paper:

Tauopathies are a class of neurodegenerative conditions, such as Alzheimer's disease, that disrupt the function of neurons and lead to a vast array of neurological changes. Tau is a microtubule associated protein that stabilizes the cytoskeleton of cells, including neurons. In tauopathies, however, these proteins can be modified abnormally and cause a wide range of issues that ultimately lead to the cell's death. Pathogenic tau has been associated with several nuclear abnormalities like nuclear envelope invaginations that, if understood, could explain the wide ranging cellular effects of pathogenic tau. In BE(2)-C neuroblastoma cells with doxycycline inducible pathological tau, many actin binding proteins were found to have increased expression. Of these, the emerin protein had a significant 2.8 fold increase compared to a control in both immunofluorescence and western blot. Emerin is a protein found in the nuclear envelope that is involved in both the cytoskeleton and nucleoskeleton. It has been found to localize to the inner nuclear membrane, where it can take part in modulating gene expression, highlighting its potential to be a protein that is affected by pathological tau and cause cell wide effects. The research presented suggests that pathogenic tau increases expression of the emerin protein, raising questions about how this can affect the nuclear and cellular structure in tauopathy afflicted neurons. Further research will be focused on understanding how increased emerin levels can relate to cell death and exploring pathological tau's impact on emerin in patient derived IPSCs. More work can also be done on how emerin overexpression may relate to other features of tauopathies, such as retrotransposon activation and the communicable nature of pathogenic tau.

Source:

Brown / Undergraduate Research in the Frost Lab

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Co-authors:

Satvik Paduri