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| Figure 2: Protein folding pathways can prove to be detrimental when the chaperone folding machinery fails to properly process an aberrant aggregationprone client protein. Under the condition of Hsp90 inhibition, Hsp90 is removed from the unproductive folding equation, disrupting this pro-aggregation pathway. Also, inhibition of Hsp90 induces the HSPs, including Hsp70. Increased levels of Hsp70 can facilitate a higher incident of interaction between client and pro-degradation pathway. As an example, interaction of a client with an ubiquitin ligase promotes proteasomal degradation of aberrant clients rather than accumulation and aggregation. |
