HDAC6, as one of the Zn 2+ -dependent Class IIb members, can regulate various biological processes via its deacetylation activity on acetylated lysines in non-histone proteins, such as cellular proliferation, motility, apoptosis, DNA damage response, activation of heat shock response, transcriptional repression as well as metabolic response. Beyond deacetylation, HDAC6 can also contribute to cellular processes like protecting against stress-induced protein aggregation and facilitating the transport of ubiquitinated proteins via the zinc-finger ubiquitin-binding domain (UBD) and a dynein-binding domain in its structure. Since HDAC6 participates in several biological processes via different enzymological and non-enzymological functions, the continuous development of inhibitors and degraders for HDAC6 has emerged as a hot topic . HDAC10, the other member of class IIb, functions as a potent polyamine deacetylase with a notable preference for N -acetylspermidine hydrolysis over acetylated lysine. Importantly, HDAC10 plays a significant role in various biological processes related to cancer, such as cellular proliferation, apoptosis, invasion, autophagy, and drug resistance. Notably, its involvement in promoting cellular survival through autophagy has been reported in neuroblastoma. In terms of drug resistance, elevated HDAC10 levels have been associated with protecting cancer cells from chemotherapy, and HDAC10 inhibition has been reported to increase cancer cell sensitivity to chemotherapy. These findings underscore the potential of HDAC10 as a promising therapeutic target in cancer treatment.