Abstract
The special class IIb histone deacetylase, HDAC6, plays a prominent role in many cellular processes related to cancer, including oncogenesis, the cell stress response, motility, and myriad signaling pathways. Many of the lessons learned from other cancers can be applied to ovarian cancer as well. HDAC6 interacts with diverse proteins such as HSP90, cortactin, tubulin, dynein, p300, Bax, and GRK2 in both the nucleus and cytoplasm to carry out these cancerous functions. Not all pro-cancer interactions of HDAC6 involve deacetylation. The idea of using HDAC6 as a target for cancer treatment continues to expand in recent years, and more potent and specific HDAC6 inhibitors are required to effectively down-regulate the tumor-prone cell signaling pathways responsible for ovarian cancer.
Highlights
Histone acetyltransferases (HATs) and deacetylases (HDACs) have opposing effects on the acetylation status of their substrates, which include core histones and non-histone proteins
We found that HDAC6 protein levels are elevated in a panel of ovarian cancer tissue samples compared with the benign samples, suggesting that HDAC6 may play a critical role in ovarian cancer development
It can bind to the polyubiquitinated misfolded proteins and the dynein motors, acting as a link between them as they are moved to the aggresomes [15,47]
Summary
Histone acetyltransferases (HATs) and deacetylases (HDACs) have opposing effects on the acetylation status of their substrates, which include core histones and non-histone proteins. HDACs may be a misnomer since they deacetylate more substrates than just the histones in the nucleus. HDACs take off an acetyl group from their substrate, including the histones of chromatin. One unique characteristic of the HDACs is their ability to shuttle between the cytoplasm and the nucleus Because of this shuttling capacity, it was soon discovered that they act on more than just histones [4]. HDACs catalyze the deacetylation of lysine residues in the N-terminal tails of histones and other substrates [6]. HDAC6 has an ubiquitin-binding zinc finger [12,13], a nuclear localization signal, a nuclear export signal, and a tetradecapeptide repeat domain [14]. The tetradecapetide repeat domain of HDAC6 presents only in the human ortholog, but not in the mouse. HDAC6 interacts with cortactin, which helps regulate cell motility [18]
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