title: Putative role of SUMOylation in controlling the activity of deubiquitinating enzymes in cancer.
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.
authors.affiliation: Department of Laboratory Medicine, Medicon Village, Lund University, 22381 Lund, Sweden.
authors.forename: Katarzyna C
authors.initials: KC
authors.lastname: Masoumi
authors.affiliation: Departament de Genètica, Facultat de Biologia, Universitat de Barcelona, 08028 Barcelona, Spain.|Institut de Biomedicina (IBUB), Universitat de Barcelona, 08007 Barcelona, Spain.|CIBERER, Instituto de Salud Carlos III, Barcelona, Spain.
authors.forename: Gemma
authors.initials: G
authors.lastname: Marfany
authors.affiliation: Department of Pathophysiology, Chemical Biology Division of Shanghai Universities E-Institutes, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
authors.forename: Yingli
authors.initials: Y
authors.lastname: Wu
authors.affiliation: Department of Laboratory Medicine, Medicon Village, Lund University, 22381 Lund, Sweden.
authors.forename: Ramin
authors.initials: R
authors.lastname: Massoumi
mesh_terms: D000818:Animals; D000067699:Ataxin-3 / Q000378:metabolism; D000074749:Deubiquitinating Enzyme CYLD; D006801:Humans; D009369:Neoplasms / Q000201:enzymology / Q000378:metabolism* / Q000473:pathology; D058207:Sumoylation; D025521:Tumor Suppressor Proteins / Q000378:metabolism; D043222:Ubiquitin Thiolesterase / Q000378:metabolism; D054875:Ubiquitination
chemical_list: D025521:Tumor Suppressor Proteins; D000067699:Ataxin-3; C409984:CYLD protein, human; D000074749:Deubiquitinating Enzyme CYLD; D043222:Ubiquitin Thiolesterase
keywords: CYLD; SUMOylation; USP25; USP28; USP39; ataxin-3; deubiquitination