Journal
AAPS JOURNAL
Volume 20, Issue 6, Pages -Publisher
SPRINGER
DOI: 10.1208/s12248-018-0254-1
Keywords
autophagy; heat shock proteins; protein quality control; ubiquitin proteasome system; unfolded protein response
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Funding
- American Cancer Society [125618-RSG-14-067-01-TBE]
- Department of Defense Ovarian Cancer Research Program [W81XWH-10-1-0386]
- American Cancer Society-Kirby Foundation Postdoctoral Fellowship [PF-17-241-01-CCG]
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Genomic aberrations inside malignant cells through copy number alterations, aneuploidy, and mutations can exacerbate misfolded and unfolded protein burden resulting in increased proteotoxic stress. Increased proteotoxic stress can be deleterious to malignant cells; therefore, these cells rely heavily on the protein quality control mechanisms for survival and proliferation. Components of the protein quality control, such as the unfolded protein response, heat shock proteins, autophagy, and the ubiquitin proteasome system, orchestrate a cascade of downstream events that allow the mitigation of the proteotoxic stress. This dependency makes components of the protein quality control mechanisms attractive targets in cancer therapeutics. In this review, we explore the components of the protein homeostasis especially focusing on the emerging cancer therapeutic agents/targets that are being actively pursued actively.
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