Chemical biology of protein citrullination by the protein A arginine deiminases.
Animals
Arginine
/ chemistry
Autoimmune Diseases
/ metabolism
Catalysis
Citrullination
Citrulline
/ chemistry
Epigenesis, Genetic
Humans
Neoplasms
/ metabolism
Neurodegenerative Diseases
/ metabolism
Protein Binding
Protein Conformation
Protein Processing, Post-Translational
Protein-Arginine Deiminases
/ metabolism
Proteins
/ chemistry
Activity-based protein profiling
Autocitrullination
Citrulline incorporation
Inhibitor
Post-translational modifications
Protein arginine deiminase (PAD)
Journal
Current opinion in chemical biology
ISSN: 1879-0402
Titre abrégé: Curr Opin Chem Biol
Pays: England
ID NLM: 9811312
Informations de publication
Date de publication:
08 2021
08 2021
Historique:
received:
01
12
2020
revised:
19
01
2021
accepted:
31
01
2021
pubmed:
7
3
2021
medline:
23
11
2021
entrez:
6
3
2021
Statut:
ppublish
Résumé
Citrullination is a post-translational modification (PTM) that converts peptidyl-arginine into peptidyl-citrulline; citrullination is catalyzed by the protein arginine deiminases (PADs). This PTM is associated with several physiological processes, including the epigenetic regulation of gene expression, neutrophil extracellular trap formation, and DNA-damage induced apoptosis. Notably, aberrant protein citrullination is relevant to several autoimmune and neurodegenerative diseases and certain forms of cancer. As such, the PADs are promising therapeutic targets. In this review, we discuss recent advances in the development of PAD inhibitors and activity-based probes, the development and use of citrulline-specific probes in chemoproteomic applications, and methods to site-specifically incorporate citrulline into proteins.
Identifiants
pubmed: 33676233
pii: S1367-5931(21)00010-7
doi: 10.1016/j.cbpa.2021.01.010
pmc: PMC8384633
mid: NIHMS1672356
pii:
doi:
Substances chimiques
Proteins
0
Citrulline
29VT07BGDA
Arginine
94ZLA3W45F
Protein-Arginine Deiminases
EC 3.5.3.15
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
19-27Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM118112
Pays : United States
Informations de copyright
Copyright © 2021 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: P.R.T. is a co–founder of Padlock Therapeutics and is entitled to payments from Bristol Myers Squibb if certain milestones are met. P.R.T. is a consultant for Related Sciences VC.
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