We find that HDAC6 and AKT physically interact with each other in the neuronal cells.
In summary, we report our finding that HDAC6 deacetylase modulates AKT activity in human neuronal cells. AKT is
acetylated at Lys163 and Lys377 in the presence of an HDAC6
inhibitor, and these residues are different from acetylation sites
modulated by SIRT1 and SIRT2. HDAC6 inhibition resulted in
decreased ability of AKT to bind PIP3 and decreased ability to
phosphorylate downstream targets, even in the presence of
Ser473 phosphorylation, which usually potentiates AKT activity.