Ubiquitination: Friend and foe in cancer

Journal article


Mansour, M.A. (2018). Ubiquitination: Friend and foe in cancer. The international journal of biochemistry & cell biology. 101, pp. 80-93. https://doi.org/10.1016/j.biocel.2018.06.001
AuthorsMansour, M.A.
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.

Year2018
JournalThe international journal of biochemistry & cell biology
Journal citation101, pp. 80-93
PublisherElsevier
Digital Object Identifier (DOI)https://doi.org/10.1016/j.biocel.2018.06.001
Publication dates
Print01 Jun 2018
Publication process dates
Accepted01 Jun 2018
Deposited10 Aug 2020
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