Tau is a neuronal protein that plays a direct or indirect role in various neuronal functions. Dysfunctions in tau can lead to neurodegenerative disorders, known as tauopathies, with Alzheimer’s disease being the most significant. Tau’s functions are influenced by its subcellular localization and its binding to specific neuronal components. Our objective is to analyze these known tau functions and explore potential new ones.

We have examined the structural and functional differences between human and mouse tau proteins, focusing on an extra amino acid sequence unique to human tau, which plays a role in axonal transport of certain proteins. Additionally, we have studied the mechanism responsible for extracellular tau secretion and tau’s involvement in localizing NMDA extrasynaptic receptors. Given that tau is a phosphoprotein primarily modified by the GSK3β kinase, we have also investigated the effects of GSK3β overexpression in neuronal cells. In Dr. Hernández’s group, we analyzed tau’s presence in glial cells (oligodendrocytes, astrocytes, and microglia) and discovered that various cell surface receptors may facilitate interactions between extracellular tau and neurons or glial cells.

Our group has collaborated extensively with other research teams, both within and outside of the CBM, on topics related to Alzheimer’s disease, other neurodegenerative disorders, and aging. Regarding aging, we have documented the rejuvenation of certain aged granule neurons in the hippocampal region following expression of reprogramming (Yamanaka) factors.