Molecular Chaperone Dysfunction in Neurodegenerative Diseases and Effects of Curcumin

Figure 3

Schematic diagram of role of HSP90 and its cochaperones and client proteins in protein folding and degradation. (a) With the help of cochaperones, clients, and proteins with a TRP domain, HSP90 maintains protein quality control, cell cycle growth, development, and other essential activities of the cell. (b) Structural changes of HSP90 during protein folding and degradation. HSP90 dynamically changes from “open” to close structures. In its open form, it can bind with misfolded proteins along with other chaperones (early complex) and become a “closed” structure (mature complex). After releasing misfolded protein for proteasomal degradation, it goes to an “open” form (HSP90 free complex).

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