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

Soung-Hun Roh1, Moses Kasembeli2, Deenadayalan Bakthavatsalam3

  • 1Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA. sroh@bcm.edu.

International Journal of Molecular Sciences
|November 13, 2015
PubMed

Insights

Molecular chaperones, including HSP70, HSP90, and the T-complex protein-1 ring complex (TRiC/CCT), are crucial for protein health and implicated in cancer development. Understanding TRiC’s role in cancer offers new therapeutic strategies.

Area of Science:

  • Molecular biology
  • Cellular biology
  • Oncology

Background:

  • Protein homeostasis, involving folding and maintenance, is vital for cell survival.
  • Molecular chaperones regulate protein folding, localization, and degradation.
  • Chaperone clients include key regulators of cell growth, suggesting a role in oncogenesis.

Purpose of the Study:

  • To review the role of chaperones, specifically HSP70 and HSP90, in cancer.
  • To highlight the emerging role of the chaperonin TRiC/CCT in cancer development and progression.
  • To explore how TRiC interacts with oncogenic clients to influence cancer cell biology.

Main Methods:

  • Literature review of existing studies on molecular chaperones and cancer.
  • Analysis of the known functions of HSP70, HSP90, and TRiC/CCT.
  • Examination of the interactions between TRiC and oncogenic proteins.

Main Results:

  • HSP70 and HSP90 are established players in various cancers.
  • TRiC/CCT is increasingly recognized for its involvement in cancer.
  • TRiC/CCT interacts with oncogenic clients, affecting growth deregulation, apoptosis, and genome instability.

Conclusions:

  • Chaperones, particularly TRiC/CCT, are significant in cancer pathogenesis.
  • Targeting TRiC's interaction with oncogenic clients presents a promising avenue for novel cancer therapies.
  • Further elucidation of TRiC's mechanisms in cancer is needed for therapeutic development.
Keywords:
HSP70/90TRiC/CCTchaperonechaperoninoncogenesisoncoproteinprotein-foldingproteostasis

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