The present investigation revealed that tau possesses pyruvate kinase activity. This kinase activity generates ATP to facilitate the transposition of telomere fragments to promoters/enhancers. The phosphorylation and dephosphorylation of tau D13 and G682 significantly influence the pyruvate kinase catalytic activity. The phosphorylation of glucagon stops pyruvate kinase activity. If pyruvate kinase activity is lost, blood glucose levels may temporarily rise. To expedite the conversion of glucose into energy, it should inhibit pyruvate kinase when glucose concentration decreases and activate it when glucose concentration increases. Thus, hypoglycemia may result in the inactivation of the tau protein's aging machinery, which inhibits pyruvate kinase activity. This could potentially lead to issues with tau protein aggregation, as supported by the previously mentioned literature.