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

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...

Full description

Bibliographic Details
Main Authors:	Roh, Soung-Hun, Kasembeli, Moses, Bakthavatsalam, Deenadayalan, Chiu, Wah, Tweardy, David J.
Format:	Online
Language:	English
Published:	MDPI 2015
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4661834/

id	pubmed-4661834
recordtype	oai_dc
spelling	pubmed-46618342015-12-10 Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis Roh, Soung-Hun Kasembeli, Moses Bakthavatsalam, Deenadayalan Chiu, Wah Tweardy, David J. Review 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. MDPI 2015-11-06 /pmc/articles/PMC4661834/ /pubmed/26561808 http://dx.doi.org/10.3390/ijms161125975 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons by Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Roh, Soung-Hun Kasembeli, Moses Bakthavatsalam, Deenadayalan Chiu, Wah Tweardy, David J.
spellingShingle	Roh, Soung-Hun Kasembeli, Moses Bakthavatsalam, Deenadayalan Chiu, Wah Tweardy, David J. Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis
author_facet	Roh, Soung-Hun Kasembeli, Moses Bakthavatsalam, Deenadayalan Chiu, Wah Tweardy, David J.
author_sort	Roh, Soung-Hun
title	Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis
title_short	Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis
title_full	Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis
title_fullStr	Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis
title_full_unstemmed	Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis
title_sort	contribution of the type ii chaperonin, tric/cct, to oncogenesis
description	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.
publisher	MDPI
publishDate	2015
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4661834/
_version_	1613506901983625216

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

Similar Items