Title

Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein.

Journal

Journal of Alzheimer's disease : JAD

Volume

17

Issue

None

Pages

319-25

Date

2009-01-01

Authors

Lim F | Santa-Maria I | Avila J | Perez M | Tortosa E | Moreno F

Figure 5 shows the presence of fibrillar polymers when the Hsp90 was mixed with tau protein. These filaments are similar to tau aggregates assembled in the presence of quinones [19] such as juglone, used here as a positive control (Fig. 5C). No filaments were observed in control samples of tau2R alone (Fig. 5A) or Hsp90 alone (data not shown).

This result suggests that the VQIVYK peptide plays a role in the interaction between Hsp90 and tau protein, a hypothesis which is also supported by the fact that a tau variant deleted for the peptide VQIVYK was unable to interact with Hsp90 under immunoprecipitation conditions (Fig. 2B).

To test the effect of Hsp90 on tau phosphorylation, this protein was mixed with tau protein in the presence of GSK-3 and ATP. Figure 4 shows that tau phosphorylation increases in the presence of increased added amounts of Hsp90.

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