[HTML][HTML] Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone …
P Bali, M Pranpat, J Bradner, M Balasis… - Journal of Biological …, 2005 - ASBMB
The hydroxamic acid (HAA) analogue pan-histone deacetylase (HDAC) inhibitors (HDIs)
LAQ824 and LBH589 have been shown to induce acetylation and inhibit the ATP binding
and chaperone function of heat shock protein (HSP) 90. This promotes the polyubiquitylation
and degradation of the pro-growth and pro-survival client proteins Bcr-Abl, mutant FLT-3, c-
Raf, and AKT in human leukemia cells. HDAC6 is a member of the class IIB HDACs. It is
predominantly cytosolic, microtubule-associated α-tubulin deacetylase that is also known to …
LAQ824 and LBH589 have been shown to induce acetylation and inhibit the ATP binding
and chaperone function of heat shock protein (HSP) 90. This promotes the polyubiquitylation
and degradation of the pro-growth and pro-survival client proteins Bcr-Abl, mutant FLT-3, c-
Raf, and AKT in human leukemia cells. HDAC6 is a member of the class IIB HDACs. It is
predominantly cytosolic, microtubule-associated α-tubulin deacetylase that is also known to …
