Putative role of SUMOylation in controlling the activity of deubiquitinating enzymes in cancer.

Summary, in English

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.

• Author: Katarzyna Masoumi; Gemma Marfany; Yingli Wu; Ramin Massoumi
• Department/s: Division of Translational Cancer Research; BioCARE: Biomarkers in Cancer Medicine improving Health Care, Education and Innovation
• Publishing year: 2016-01-18
• Language: English
• Pages: 565-574
• Publication/Series: Future Oncology
• Volume: 12
• Issue: 4
• Links: http://www.ncbi.nlm.nih.gov/pubmed/26777062?dopt=Abstract; http://dx.doi.org/10.2217/fon.15.320
• Document type: Journal article review
• Publisher: Future Medicine Ltd.
• Topic: Cancer and Oncology
• Status: Published
• ISBN/ISSN/Other: ISSN: 1479-6694