title: Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis.
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA. sroh@bcm.edu.
authors.forename: Soung-Hun
authors.initials: SH
authors.lastname: Roh
authors.affiliation: Division of Internal Medicine, the University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA. mmkasembeli@mdanderson.org.
authors.forename: Moses
authors.initials: M
authors.lastname: Kasembeli
authors.affiliation: Department of Molecular Cardiology, Texas Heart Institute, Houston, TX 77030, USA. dbakthavatsalam@texasheart.org.
authors.forename: Deenadayalan
authors.initials: D
authors.lastname: Bakthavatsalam
authors.affiliation: Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA. wah@bcm.edu.
authors.forename: Wah
authors.initials: W
authors.lastname: Chiu
authors.affiliation: Division of Internal Medicine, the University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA. djtweardy@mdanderson.org.
authors.forename: David J
authors.initials: DJ
authors.lastname: Tweardy
mesh_terms: D017209:Apoptosis; D063646:Carcinogenesis / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D056404:Chaperonin Containing TCP-1 / Q000235:genetics* / Q000378:metabolism; D018450:Disease Progression; D015972:Gene Expression Regulation, Neoplastic; D042822:Genomic Instability; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D018841:HSP90 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D009363:Neoplasm Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D009369:Neoplasms / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D011487:Protein Conformation; D017510:Protein Folding; D015398:Signal Transduction
chemical_list: D018840:HSP70 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D009363:Neoplasm Proteins; D056404:Chaperonin Containing TCP-1
keywords: HSP70/90; TRiC/CCT; chaperone; chaperonin; oncogenesis; oncoprotein; protein-folding; proteostasis