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

Masoumi, Katarzyna LU ; Marfany, Gemma; Wu, Yingli and Massoumi, Ramin LU (2016) In Future Oncology 12(4). p.565-574
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Future Oncology
volume
12
issue
4
pages
565 - 574
publisher
Future Medicine Ltd.
external identifiers
  • pmid:26777062
  • scopus:84957631162
  • wos:000369525700015
ISSN
1479-6694
DOI
10.2217/fon.15.320
language
English
LU publication?
yes
id
9d7fc8ce-92a3-47b9-958f-3c748a0be7c3 (old id 8577352)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/26777062?dopt=Abstract
date added to LUP
2016-02-03 17:50:29
date last changed
2017-05-11 15:33:14
@article{9d7fc8ce-92a3-47b9-958f-3c748a0be7c3,
  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.},
  author       = {Masoumi, Katarzyna and Marfany, Gemma and Wu, Yingli and Massoumi, Ramin},
  issn         = {1479-6694},
  language     = {eng},
  month        = {01},
  number       = {4},
  pages        = {565--574},
  publisher    = {Future Medicine Ltd.},
  series       = {Future Oncology},
  title        = {Putative role of SUMOylation in controlling the activity of deubiquitinating enzymes in cancer.},
  url          = {http://dx.doi.org/10.2217/fon.15.320},
  volume       = {12},
  year         = {2016},
}