Abstract
Targeting the ubiquitin-proteasome pathway gained more attention as a rational approach in the treatment of human cancer. The 26S proteasome (2000-kDa) complex, which degrades ubiquitinated proteins, contains in addition to the 20S proteasome a 19S regulatory complex composed of multiple ATP ases and components necessary for binding protein substrates. Accordingly, proteasome is considered an exciting target for the development of anticancer therapies. Inhibition of proteasome machinery has shown a positive clinical benefit for cancer patients. Thus, the highlight of the mechanistic role of proteasome regulators, both inhibitors and activators, may help to improve the outcome of tumor treatment. In this review, we will focus on the molecular action of proteasome regulators in tumor treatment.
Highlights
The ubiquitin-proteasome system (UPS) is a conserved pathway responsible for the selective degradation of the majority of nuclear and cytosolic proteins in normal and tumor cells
The ubiquitin-proteasome pathway plays an essential role in cellular homeostasis [8], and the levels of proteasome activity in cancer cells are higher when compared with normal cells [9]
The discovery of the ubiquitin-proteasome pathway opened a new era for tumor therapy
Summary
The ubiquitin-proteasome system (UPS) is a conserved pathway responsible for the selective degradation of the majority of nuclear and cytosolic proteins in normal and tumor cells. Because of the importance of the proteasome in common cellular functions such as, protein turnover, DNA repair, and intracellular trafficking [10,11,12,13], inhibition or activation of the proteasome is considered as an ideal therapeutic strategies for a variety of diseases including, cancer.
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