Abstract
PA28γ is a nuclear activator of the 20S proteasome, which is involved in the regulation of several essential cellular processes and angiogenesis. Over the past 20 years, many amino acid sites and motifs have been proven to play important roles in the characteristic functions of PA28γ. The number of binding partners and validated cellular functions of PA28γ have increased, which has facilitated the clarification of its involvement in different biological events. PA28γ is involved in the progression of various diseases, and its aberrant overexpression in cancer is remarkable. Patients with low levels of PA28γ expression have a higher survival rate than those with high levels of PA28γ expression, as has been shown for a wide variety of tumors. The functions of PA28γ in cancer can be divided into five main categories: cell proliferation, cell apoptosis, metastasis and invasion, cell nuclear dynamics that have relevance to angiogenesis, and viral infection. In this review, we focus on the role of PA28γ in cancer, summarizing its aberrant expression, prooncogenic effects and underlying mechanisms in various cancers, and we highlight the possible cancer-related applications of PA28γ, such as its potential use in the diagnosis, targeted treatment and prognostic assessment of cancer.
Highlights
The proteasome system is an indispensable protein degradation system that has the responsibility of degrading the majority of the proteins in eukaryotes [1, 2]
proteasome activator 28a (PA28a) and proteasome activator 28b (PA28b) are only found in vertebrates, while proteasome activator 28g (PA28g) has been found in both vertebrates and invertebrates and is more highly conserved [6]
Another difference is that the expression levels of both PA28a and PA28b can be enhanced by interferon-g (IFN-g) induction, and they take part in the formation of the hybrid proteasome 19S-20S-11S while there’s no clear evidence that PA28g can form hybrid proteasomes [5]
Summary
The proteasome system is an indispensable protein degradation system that has the responsibility of degrading the majority of the proteins in eukaryotes [1, 2]. The results showed that most of the cancer samples had higher levels of PA28g than the adjacent tissues except in kidney chromophobe and kidney renal clear cell carcinoma. The Mechanism of PA28g Regulate the Cell Cycle and Apoptosis
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