期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 16, 期 11, 页码 26706-26720出版社
MDPI
DOI: 10.3390/ijms161125975
关键词
protein-folding; proteostasis; oncogenesis; chaperone; chaperonin; HSP70; 90; TRiC; CCT; oncoprotein
资金
- NIH [P41GM103832, PN2EY016525]
- Cancer Prevention and Research Institute of Texas [RP110291]
The folding of newly synthesized proteins and the maintenance of pre-existing proteins are essential in sustaining a living cell. A network of molecular chaperones tightly guides the folding, intracellular localization, and proteolytic turnover of proteins. Many of the key regulators of cell growth and differentiation have been identified as clients of molecular chaperones, which implies that chaperones are potential mediators of oncogenesis. In this review, we briefly provide an overview of the role of chaperones, including HSP70 and HSP90, in cancer. We further summarize and highlight the emerging the role of chaperonin TRiC (T-complex protein-1 ring complex, also known as CCT) in the development and progression of cancer mediated through its critical interactions with oncogenic clients that modulate growth deregulation, apoptosis, and genome instability in cancer cells. Elucidation of how TRiC modulates the folding and function of oncogenic clients will provide strategies for developing novel cancer therapies.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据