Knockdown of KAT5/KIF11 induces autophagy and promotes apoptosis in anaplastic thyroid cancer cells.

K (lysine) acetyltransferase (KAT) 5, which is a member of the KAT family of enzymes, has been found to act as a regulatory factor in various types of cancer. However, the role of KAT5 in anaplastic thyroid carcinoma (ATC) and its underlying mechanism is still elusive. The expression levels of KAT5 and kinesin family member 11 (KIF11) in ATC cells were assessed utilizing reverse transcription-quantitative PCR and western blot analyses. The cell proliferative ability was assessed via Cell Counting Kit-8 assay and using 5-ethynyl-2'-deoxyuridine staining. Flow cytometry and western blot analyses were applied for the assessment of cell apoptosis. Cell autophagy was investigated by employing western blot analysis and immunofluorescence staining. In addition, the enrichment of histone H3 lysine 27 acetylation (H3K27ac) and RNA polymerase II (RNA pol II) was analyzed by chromatin immunoprecipitation assay. It was shown that KAT5 expression was markedly increased in ATC cells. KAT5 depletion suppressed the cell proliferative capability but promoted the induction of apoptosis and autophagy. In addition, the autophagy inhibitor 3-methyladenine reversed the effects of KAT5 deficiency on the proliferative and apoptotic activities of 8505C cells. With regard to the mechanism, it was found that KAT5 inhibited the expression of KIF11 by repressing the enrichment of H3K27ac and RNA pol II. Upregulation of KIF11 expression reversed the effects of KAT5 silencing on the proliferative activity, apoptosis and autophagy of 8505C cells. In conclusion, the results indicated that KAT5 induced autophagy and promoted apoptosis of ATC cells by targeting KIF11, which may provide a promising target for the treatment of ATC.