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Ubiquitination: friend and foe in cancer

Ubiquitination: friend and foe in cancer
Ubiquitination: friend and foe in cancer
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.
80-93
Mansour, Mohammed
03d901e1-959e-4c7d-acc6-33c6a4b129f7
Mansour, Mohammed
03d901e1-959e-4c7d-acc6-33c6a4b129f7

Mansour, Mohammed (2018) Ubiquitination: friend and foe in cancer. The International Journal of Biochemistry & Cell Biology, 101, 80-93.

Record type: Article

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.

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Accepted/In Press date: 1 June 2018
e-pub ahead of print date: 1 June 2018

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Local EPrints ID: 432559
URI: https://eprints.soton.ac.uk/id/eprint/432559
PURE UUID: 1aff9725-72fc-4c79-9549-4c29751e1d30

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Date deposited: 18 Jul 2019 16:30
Last modified: 18 Jul 2019 16:30

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