Putative role of SUMOylation in controlling the activity of deubiquitinating enzymes in cancer.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8577352
- author
- Masoumi, Katarzyna LU ; Marfany, Gemma ; Wu, Yingli and Massoumi, Ramin LU
- organization
- publishing date
- 2016-01-18
- 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
- pmid:26777062
- 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
- 2016-04-04 07:12:03
- date last changed
- 2022-04-23 07:57:07
@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}},
doi = {{10.2217/fon.15.320}},
volume = {{12}},
year = {{2016}},
}