Introduction: A predominant molecular component analyzed in the study of neurodegenerative diseases is the presence of the Tau-GSK3 β complex and its association with protein aggregation into the cell. Several evidences show that GSK3 β has an important role in abnormal pattern of the phosphorylation of Tau. However, the molecular events that are governing this complex are unknown. Aim: To determine the effect of 17 β -estradiol treatment on the expression and association of Tau hyperphosphorylation responsible kinases. Methods: 17 β -estradiol treatments were realized in the hippocampus of ovariectomized adult wistar rats and in hippocampal primary cultures treated with β -amiloid. Protein complex association was assessed by co-immunoprecipitation, toxicity assay by LDH release and cell morphologic changes by confocal microscopy. Results: Our results show that 17 β -estradiol produced dissociation of macromolecular complexes like Tau/GSK3 β , Tau /GluR2/3, Tau/FAK, and Tau/Fyn in hippocampus of adult rat. In addition the expression of GSK3 β -ptyr was decreased by the hormonal treatment and this one regulated the defosforilation of Tau in an excitotoxicity model by β -amiloid. Conclusions: It suggests new targets that will contribute to neuroprotection and neuronal plasticity studies mediated by the estrogen.