PMID- 37234921
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20240214
IS  - 2296-889X (Print)
IS  - 2296-889X (Electronic)
IS  - 2296-889X (Linking)
VI  - 10
DP  - 2023
TI  - MALDI-TOF Mass Spectrometry for interrogating ubiquitin enzymes.
PG  - 1184934
LID - 10.3389/fmolb.2023.1184934 [doi]
LID - 1184934
AB  - The attachment of ubiquitin to a substrate (ubiquitination or ubiquitylation) 
      impacts its lifetime and regulates its function within the cell. Several classes 
      of enzymes oversee the attachment of ubiquitin to the substrate: an E1 activating 
      enzyme that makes ubiquitin chemically susceptible prior to the following stages 
      of conjugation and ligation, respectively mediated by E2 conjugating enzymes 
      (E2s) and E3 ligases (E3s). Around 40 E2s and more than 600 E3s are encoded in 
      the human genome, and their combinatorial and cooperative behaviour dictate the 
      tight specificity necessary for the regulation of thousands of substrates. The 
      removal of ubiquitin is orchestrated by a network of about 100 deubiquitylating 
      enzymes (DUBs). Many cellular processes are tightly controlled by ubiquitylation, 
      which is essential in maintaining cellular homeostasis. Because of the 
      fundamental role(s) of ubiquitylation, there is an interest in better 
      understanding the function and specificity of the ubiquitin machinery. Since 
      2014, an expanding array of Matrix-assisted laser desorption/ionization 
      time-of-flight (MALDI-TOF) Mass Spectrometry (MS) assays have been developed to 
      systematically characterise the activity of a variety of ubiquitin enzymes in 
      vitro. Here we recapitulate how MALDI-TOF MS aided the in vitro characterization 
      of ubiquitin enzymes and the discovery of new and unexpected of E2s and DUBs 
      functions. Given the versatility of the MALDI-TOF MS approach, we foreseen the 
      use of this technology to further expand our understanding of ubiquitin and 
      ubiquitin-like enzymes.
CI  - Copyright (c) 2023 De Cesare.
FAU - De Cesare, Virginia
AU  - De Cesare V
AD  - MRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, 
      School of Life Sciences, University of Dundee, Dundee, United Kingdom.
LA  - eng
GR  - MR/V025759/1/MRC_/Medical Research Council/United Kingdom
PT  - Journal Article
DEP - 20230509
PL  - Switzerland
TA  - Front Mol Biosci
JT  - Frontiers in molecular biosciences
JID - 101653173
PMC - PMC10206504
OTO - NOTNLM
OT  - E2 conjugating enzyme
OT  - E3 ligase
OT  - HECT E3 ligase
OT  - Matrix-assisted laser desorption/ionization time-of-flight Mass-Spectrometry 
      (MALDI-TOF MS)
OT  - RBR E3 ligase, RING E3 ligase
OT  - deubiquinating enzymes
OT  - non-lysine ubiquitination
OT  - ubiquitin (Ub)
COIS- The author declares that the research was conducted in the absence of any 
      commercial or financial relationships that could be construed as a potential 
      conflict of interest.
EDAT- 2023/05/26 19:14
MHDA- 2023/05/26 19:15
PMCR- 2023/01/01
CRDT- 2023/05/26 12:19
PHST- 2023/03/12 00:00 [received]
PHST- 2023/04/13 00:00 [accepted]
PHST- 2023/05/26 19:15 [medline]
PHST- 2023/05/26 19:14 [pubmed]
PHST- 2023/05/26 12:19 [entrez]
PHST- 2023/01/01 00:00 [pmc-release]
AID - 1184934 [pii]
AID - 10.3389/fmolb.2023.1184934 [doi]
PST - epublish
SO  - Front Mol Biosci. 2023 May 9;10:1184934. doi: 10.3389/fmolb.2023.1184934. 
      eCollection 2023.