| Range |
~5 μM
|
| Organism |
Unspecified |
| Reference |
Theillet FX et al., Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chem Rev. 2014 Jul 9 114(13):6661-714. doi: 10.1021/cr400695p p.6676 right column 3rd paragraphPubMed ID24901537
|
| Primary Source |
[357] Karagöz GE et al., Hsp90-Tau complex reveals molecular basis for specificity in chaperone action. Cell. 2014 Feb 27 156(5):963-74. doi: 10.1016/j.cell.2014.01.037 [359] Thompson AD et al., Analysis of the tau-associated proteome reveals that exchange of Hsp70 for Hsp90 is involved in tau degradation. ACS Chem Biol. 2012 Oct 19 7(10):1677-86. doi: 10.1021/cb3002599PubMed ID24581495, 22769591
|
| Method |
Primary source [357] abstract: "Here, [investigators] obtained a structural model of Hsp90 in complex with its natural disease-associated substrate, the intrinsically disordered Tau protein." Primary source [359] abstract: "In the current study, [investigators] used one of these probes [recently identified chemical probes that markedly accelerate the clearance of tau in cellular and animal models] in combination with immunoprecipitation and mass spectrometry to identify 48 proteins whose association with tau changes during the first 10 min after treatment." |
| Comments |
P.6676 right column 3rd paragraph: "Several specific chaperone/IDP [intrinsically disordered proteins] interactions have been reported. Aggregation-prone regions of human tau for example, interact with Hsp72 and Hsc70, two homologous variants of the Hsp70 family of proteins, as well as with Hsp90 (ref 356, primary source 357). These tau sites become available and accessible only when the protein dissociates from microtubules (ref 358). In the presence of ATP, Hsp70 and Hsp90 bind tau with a dissociation-constant in the low micromolar range (∼5 μM for Hsp90) (primary sources)." |
| Entered by |
Uri M |
| ID |
116288 |