Ubiquitination: Friend and foe in cancer. (August 2018)

• Record Type: Journal Article
• Authors: Mansour, Mohammed A.
• Is Part Of: International journal of biochemistry & cell biology. Volume 101(2018)
• Page Start: 80
• Page End: 93
• Publication Date: 2018-08
• Subjects: Ub ubiquitin -- UBLs ubiquitin-like proteins -- DUBs deubiquitinating enzymes -- TCR T cell receptor -- UPS ubiquitin–proteasome system -- IAPs inhibitors of apoptosis-related proteins -- GAPs GTPase-activating proteins -- PI3K phosphatidylinositol 3-kinase -- HECT homology to E6AP C-terminus -- RING really interesting new gene -- CDK cyclin-dependent kinase -- USP ubiquitin-specific protease -- PROTACs protein-targeting chimeric molecules -- HyT hydrophobicity tags -- NF-κB nuclear factor kappa-B -- TCGA The Cancer Genome Atlas -- UCP ubiquitin carrier protein -- MMP matrix metalloprotease; ubiquitin–proteasome system -- Cancer -- E3 ligases -- MDM2 -- P53 -- SCF complex -- Deubiquitinating enzyme -- PROTAC -- Hydrophobic tag; Biochemistry -- Periodicals; Cytology -- Periodicals; Biochemistry -- Periodicals; Cell Biology -- Periodicals; Biochimie -- Périodiques; Cytologie -- Périodiques; Biochimie; Cytologie; Biochemistry; Cytology; Ressource Internet (Descripteur de forme); Périodique électronique (Descripteur de forme); Periodicals; 572.05
• DOI: 10.1016/j.biocel.2018.06.001
• Languages: English
• ISSNs: 1357-2725

Abstract

Graphical abstract: Abstract: Dynamic modulation and posttranslational modification of proteins are tightly controlled biological processes that occur in response to physiological cues. One such dynamic modulation is ubiquitination, which marks proteins for degradation via the proteasome, altering their localization, affecting their activity, and promoting or interfering with protein interactions. Hence, ubiquitination is crucial for a plethora of physiological processes, including cell survival, differentiation and innate and adaptive immunity. Similar to kinases, components of the ubiquitination system are often deregulated, leading to a variety of diseases, such as cancer and neurodegenerative disorders. In a context-dependent manner, ubiquitination can regulate both tumor-suppressing and tumor-promoting pathways in cancer. This review outlines how components of the ubiquitination systems (e.g. E3 ligases and deubiquitinases) act as oncogenes or tumor suppressors according to the nature of their substrates. Furthermore, I interrogate how the current knowledge of the differential roles of ubiquitination in cancer lead to technical advances to inhibit or reactivate the components of the ubiquitination system accordingly.