Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

p73 and tau both play roles in neurodevelopment and neurodegeneration. In this pilot study we show by Western blotting that TAp73alpha induces phosphorylation of human 2N4R tau at threonine-205 and at the PHF-1 epitope (serine366/serine404) in HEK293a cells. Neither the dominant negative isoform, DeltaNp73, nor a transcriptionally inactive mutant TAp73alpha(R292H) altered tau phosphorylation indicating that tau phosphorylation is dependent on the transcriptional activity of TAp73alpha. Consistent with this, confocal microscopy revealed that tau and TAp73alpha were spatially separated within the cell; tau being located in the cytoskeletal compartment whilst TAp73alpha was found in the nucleus. These findings have ramifications for microtubule dynamics associated with axonal growth during development and for neuronal death associated with Alzheimer's disease and other tauopathies.

Original publication




Journal article


Neurosci Lett

Publication Date





30 - 34


Alzheimer Disease, Brain, Cell Compartmentation, Cell Nucleus, Cytoskeleton, DNA-Binding Proteins, Genes, Tumor Suppressor, Genetic Predisposition to Disease, Humans, Microscopy, Confocal, Microtubules, Mutation, Nerve Degeneration, Neurons, Nuclear Proteins, Phosphorylation, Tauopathies, Transcription, Genetic, Transcriptional Activation, Tumor Protein p73, Tumor Suppressor Proteins, tau Proteins