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

Research output: Contribution to journalReview article

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.

Details

Authors
Organisations
External organisations
  • University of Barcelona
  • Shanghai Jiao Tong University
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Cancer and Oncology
Original languageEnglish
Pages (from-to)565-574
JournalFuture Oncology
Volume12
Issue number4
Early online date2016 Jan 18
Publication statusPublished - 2016
Publication categoryResearch
Peer-reviewedYes