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ABSTRACT
Deubiquitinating enzymes (DUBs) are specialized proteins that can recognize ubiquitinated proteins, and after direct interaction, deconjugate monomeric or polymeric ubiquitin chains, thus changing the fate of the substrates. This process is instrumental in mediating or changing downstream signaling pathways. Beside mutations and alterations in their expression levels, the activity and stability of deubiquitinating enzymes is vital for their function. SUMOylations consist of the conjugation of the small peptide SUMO to protein substrates which is very similar to ubiquitination in the mechanistic and machinery required. In this review, we will focus on how SUMOylation can regulate DUB enzymatic activity, stability or DUB interaction with partners and substrates, in cancer. Furthermore, we will discuss the impact of these recent findings in the identification of new potential tools for efficient anticancer treatment strategies.
Acknowledgements
G Marfany acknowledges all the present and past members of her research group for long-standing support and helpful discussions.
Financial & competing interests disclosure
R Massoumi has been funded by Swedish Cancer Foundation and by funding from the European Research Council (ERC), under the European Union’s Seventh Framework Programme for Research and Technology Development, grant agreement no. 260460. G Marfany has been funded by BFU2010-15656 and SAF2013-49069-C2-1-R (Ministerio de Ciencia e Innovación) and SGR2014-0932 (Generalitat de Catalunya). The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.
No writing assistance was utilized in the production of this manuscript.