Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis

International Journal of Molecular Sciences

Soung-Hun Roh³  Moses Kasembeli¹  Deenadayalan Bakthavatsalam²  Wah Chiu³  David J. Tweardy¹ 

[1] Division of Internal Medicine, the University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA;Department of Molecular Cardiology, Texas Heart Institute, Houston, TX 77030, USA;Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA;

关键词: protein-folding;    proteostasis;    oncogenesis;    chaperone;    chaperonin;    HSP70/90;    TRiC/CCT;    oncoprotein;   

DOI  :  10.3390/ijms161125975

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.