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Ubiquitin-modifying Enzymes as Drug Targets and Biomarkers in Cancer

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E3 ubiquitin ligases contribute to the regulatory control for a vast array of substrates and binding partners. The E3 ligases comprise the HECT, RING-finger, U-box, and PHD-finger protein families. The RING-finger family has the most members and contain ligases such as the anaphase-promoting complex (APC) and ...

E3 ubiquitin ligases contribute to the regulatory control for a vast array of substrates and binding partners. The E3 ligases comprise the HECT, RING-finger, U-box, and PHD-finger protein families. The RING-finger family has the most members and contain ligases such as the anaphase-promoting complex (APC) and the SCF complex (Skp1-Cullin-F-box protein complex), as well as many TRIM proteins. These proteins are key regulators of cell fate in both normal and malignant cell types by adding ubiquitin to proteins and are increasingly targets for pharmaceutical modulation. They are opposed to another class of enzymes referred to as deubiquitinating enzymes from protein families such as USP, UCH, OTU, JAMM, MCPIP, which also have become drug targets.

The objective of this special issue is to discuss and advance the current knowledge regarding the roles and targetability of the ubiquitination machinery, in cancer.

We welcome high-quality, original papers in both clinical and experimental research, solicited and unsolicited reviews, and commentaries. Papers could relate to specific cancers, clinical group or cancers in general. The most relevant papers will be those which focus on regulation of ubiquitination in at least one of the three key areas below:

1) as diagnostic/prognostic factors, biomarkers and/or risk factors in cancer

2) as therapeutic targets, direct targets for inhibitor development/strategies (e.g. Proteolysis
Targeting Chimeras (PROTACs), computer modelling, drug screening, drug re-purposing). These
studies must have clear significance in understanding cancer cell biology or treating cancer. PROTAC
and similar strategies could also be shown to utilize ubiquitin regulated pathways to target or better
characterise functions of significant proteins in cancer contexts.

3) as an interacting partner of a clinically significant protein, RNA or DNA in cancer/cancer models. Contexts could include, but not limited to:
a) control of transcription factor protein stability or activity (e.g. MYC, MYCN, TP53, RUNX1)
b) replication stress, DNA repair, DNA damage, R-loops (RNA:DNA hybrids), chromosome instability
c) cell cycle control, proliferation (e.g. cyclin regulation)
d) localisation of clinically significant proteins/nucleic acids
e) changes in novel protein interactions, protein-binding, DNA-binding, RNA-binding
f) cell/tumour response to established or emerging cancer therapies, differentiation therapies
(retinoic acid), death resistance, apoptosis


Keywords: e3 ubiquitin ligase, e3 ligases, PROTACs, transcription factors, deubiquitinating enzymes, TRIM proteins, Cancer targets, Prognostic factors


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

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