Highly Specialized Ubiquitin-Like Modifications: Shedding Light into the UFM1 Enigma
Post-translational modification with Ubiquitin-like proteins represents a complex signaling language regulating virtually every cellular process. Among these post-translational modifiers is Ubiquitin-fold modifier (UFM1), which is covalently attached to its substrates through the orchestrated action...
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2021-02-01
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Online Access: | https://www.mdpi.com/2218-273X/11/2/255 |
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doaj-b5a9e7fb86ad4928bcdbc77934392ef72021-02-11T00:03:29ZengMDPI AGBiomolecules2218-273X2021-02-011125525510.3390/biom11020255Highly Specialized Ubiquitin-Like Modifications: Shedding Light into the UFM1 EnigmaKatharina F. Witting0Monique P.C. Mulder1Oncode Institute and Department of Cell and Chemical Biology, Leiden University Medical Center LUMC, Einthovenweg 20, 2333 ZC Leiden, The NetherlandsOncode Institute and Department of Cell and Chemical Biology, Leiden University Medical Center LUMC, Einthovenweg 20, 2333 ZC Leiden, The NetherlandsPost-translational modification with Ubiquitin-like proteins represents a complex signaling language regulating virtually every cellular process. Among these post-translational modifiers is Ubiquitin-fold modifier (UFM1), which is covalently attached to its substrates through the orchestrated action of a dedicated enzymatic cascade. Originally identified to be involved embryonic development, its biological function remains enigmatic. Recent research reveals that UFM1 regulates a variety of cellular events ranging from DNA repair to autophagy and ER stress response implicating its involvement in a variety of diseases. Given the contribution of UFM1 to numerous pathologies, the enzymes of the UFM1 cascade represent attractive targets for pharmacological inhibition. Here we discuss the current understanding of this cryptic post-translational modification especially its contribution to disease as well as expand on the unmet needs of developing chemical and biochemical tools to dissect its role.https://www.mdpi.com/2218-273X/11/2/255UFM1Ubiquitin-like modifierssubstratesactivity-based probes |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Katharina F. Witting Monique P.C. Mulder |
spellingShingle |
Katharina F. Witting Monique P.C. Mulder Highly Specialized Ubiquitin-Like Modifications: Shedding Light into the UFM1 Enigma Biomolecules UFM1 Ubiquitin-like modifiers substrates activity-based probes |
author_facet |
Katharina F. Witting Monique P.C. Mulder |
author_sort |
Katharina F. Witting |
title |
Highly Specialized Ubiquitin-Like Modifications: Shedding Light into the UFM1 Enigma |
title_short |
Highly Specialized Ubiquitin-Like Modifications: Shedding Light into the UFM1 Enigma |
title_full |
Highly Specialized Ubiquitin-Like Modifications: Shedding Light into the UFM1 Enigma |
title_fullStr |
Highly Specialized Ubiquitin-Like Modifications: Shedding Light into the UFM1 Enigma |
title_full_unstemmed |
Highly Specialized Ubiquitin-Like Modifications: Shedding Light into the UFM1 Enigma |
title_sort |
highly specialized ubiquitin-like modifications: shedding light into the ufm1 enigma |
publisher |
MDPI AG |
series |
Biomolecules |
issn |
2218-273X |
publishDate |
2021-02-01 |
description |
Post-translational modification with Ubiquitin-like proteins represents a complex signaling language regulating virtually every cellular process. Among these post-translational modifiers is Ubiquitin-fold modifier (UFM1), which is covalently attached to its substrates through the orchestrated action of a dedicated enzymatic cascade. Originally identified to be involved embryonic development, its biological function remains enigmatic. Recent research reveals that UFM1 regulates a variety of cellular events ranging from DNA repair to autophagy and ER stress response implicating its involvement in a variety of diseases. Given the contribution of UFM1 to numerous pathologies, the enzymes of the UFM1 cascade represent attractive targets for pharmacological inhibition. Here we discuss the current understanding of this cryptic post-translational modification especially its contribution to disease as well as expand on the unmet needs of developing chemical and biochemical tools to dissect its role. |
topic |
UFM1 Ubiquitin-like modifiers substrates activity-based probes |
url |
https://www.mdpi.com/2218-273X/11/2/255 |
work_keys_str_mv |
AT katharinafwitting highlyspecializedubiquitinlikemodificationssheddinglightintotheufm1enigma AT moniquepcmulder highlyspecializedubiquitinlikemodificationssheddinglightintotheufm1enigma |
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