Figure 3: A model of how HDAC6/Hsp90 and HDAC10/Hsp70 collaboratively work as protein chaperones. Deacetylation of Hsp90 catalyzed by HDAC6 might prime its chaperone function. Deacetylated Hsp70, catalyzed by HDAC10 or by another deacetylase, joins the Hsp90/chaperone client complexes to help with correct folding of the clients. Acetylation of Hsp70, a likely result of HDAC10 deregulation, might cause incorrect folding of proteins or facilitate the subsequent degradation of misfolded proteins.