p(SFAM:"HSP90 Family")

Entity

Name

HSP90 Family

Namespace

SFAM

Namespace Version

20170725

Namespace URL

https://arty.scai.fraunhofer.de/artifactory/bel/namespace/selventa-protein-families/selventa-protein-families-20170725.belns

Previous work showed that Hsp90 inhibition with 17-AAG reduced phospho-tau levels in vivo (16, 23). We speculated that Cdc37 might modulate Hsp90 inhibitor efficacy for phosphotau. M17 cells were transfected with Cdc37 siRNA and then treated with 1 μM 17-AAG for 24 h. Indeed, reducing Cdc37 synergized with Hsp90 inhibition to reduce tau levels more potently than either condition alone (Fig. 6A). PubMed:21367866

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). PubMed:19363271

Previous work showed that Hsp90 inhibition with 17-AAG reduced phospho-tau levels in vivo (16, 23). We speculated that Cdc37 might modulate Hsp90 inhibitor efficacy for phosphotau. M17 cells were transfected with Cdc37 siRNA and then treated with 1 μM 17-AAG for 24 h. Indeed, reducing Cdc37 synergized with Hsp90 inhibition to reduce tau levels more potently than either condition alone (Fig. 6A). PubMed:21367866

This coordination of kinase triage decisions by Hsp90 requires the co-chaperone Cdc37 (cell division cycle protein 37). The Hsp90/Cdc37 machine is essential for the maturation of a number of kinases, including Akt PubMed:21367866

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. PubMed:19363271

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). PubMed:19363271

In addition to its peptidyl–prolyl isomerase activity, FKBP52 serves as a molecular chaperone. This activity depends on its tetratricopeptide repeat domain (27) to which the molecular chaperone HSP90 and other proteins bind. PubMed:20133804

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). PubMed:19363271

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). PubMed:19363271

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. PubMed:19363271

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). PubMed:19363271

In addition to its peptidyl–prolyl isomerase activity, FKBP52 serves as a molecular chaperone. This activity depends on its tetratricopeptide repeat domain (27) to which the molecular chaperone HSP90 and other proteins bind. PubMed:20133804

This coordination of kinase triage decisions by Hsp90 requires the co-chaperone Cdc37 (cell division cycle protein 37). The Hsp90/Cdc37 machine is essential for the maturation of a number of kinases, including Akt PubMed:21367866

Previous work showed that Hsp90 inhibition with 17-AAG reduced phospho-tau levels in vivo (16, 23). We speculated that Cdc37 might modulate Hsp90 inhibitor efficacy for phosphotau. M17 cells were transfected with Cdc37 siRNA and then treated with 1 μM 17-AAG for 24 h. Indeed, reducing Cdc37 synergized with Hsp90 inhibition to reduce tau levels more potently than either condition alone (Fig. 6A). PubMed:21367866